the 53rd enc - enc conference · on behalf of the organizing committee, welcome to the 53rd enc!...

TTThhheee 555333rrrddd EEENNNCCC Experimental Nuclear Magnetic Resonance Conference April 15 - 20, 2012 Miami, Florida

Executive Committee Chair A.J. Shaka Univ. of California, Irvine

Treasurer Joseph A. Helpern Med. Univ. of S. Carolina

Secretary Tatyana Polenova University of Delaware

Chair Elect Michael Garwood University of Minnesota

Past Chair Lyndon Emsley Ecole Norm. Sup. de Lyon Marc Baldus Utrecht University Rafael Bruschweiler Florida State University Teresa Carlomagno EMBL Heidelberg Frank Engelke Bruker Biospin Philip J. Grandinetti Ohio State University Sangi Han Univ. of CA Santa Barbara Eriks Kupce Varian, Ltd. J. Patrick Loria Yale University Istvan Pelczer Princeton University James Prestegard University of Georgia Chad M. Rienstra University of Illinois Dieter Suter Universität Dortmund Daniel B. Vigneron Univ. of CA, San Francisco Yulan Wang Wuhan Institute

Conference Managers Judith A. Sjoberg Jennifer Watson Cindi Lilly A/V Coordinator Dean Willingham

On behalf of the organizing committee, welcome to the 53rd ENC! The program features the kind of eclectic, groundbreaking science in magnetic resonance that I know will make it a memorable and enlightening intellectual experience. You can expect the range of fundamental methods mixed with cutting-edge applications that make the ENC unique. We support a large number of students through travel stipends and are especially grateful to Suraj Manrao, who contributes substantially to the stipend fund. We have listed the large number of students whom he personally supports in this program. Hotel rooms have free in-room Internet and there is free WiFi

throughout the meeting area. The Welcome Reception on Sunday will feature a Latin Buffet, and will be a great way to meet and greet your ENC friends and colleagues. Nobel Laureate Richard Ernst is our after-dinner speaker on Thursday evening. Don’t miss this unique opportunity to rediscover the historical development of FT and 2D NMR. This program is open to all. I hope you will also attend the Banquet Dinner. If you do not have a ticket, they are still available at the conference registration desk. Our corporate partners have planned some exceptional hospitality suite food and entertainment for you, as well as displays of the latest and best products. Finally, be sure to visit the exhibit booths just outside the session ballroom. Enjoy beautiful Miami! A. J. Shaka Chair, 53rd ENC

TABLE OF CONTENTS General Information .......................................... 2 Awards .............................................................. 3 In Memoriam ..................................................... 6 Corporate Sponsors/Media Partners ................ 7 Hospitality Suites/Exhibitors ............................. 9 Hotel Floor Plan .............................................. 10 Program Overview .......................................... 11 Sunday/Monday Program ............................... 12 Tuesday Program ........................................... 14 Wednesday Program ...................................... 17 Thursday Program .......................................... 20 Friday Program ............................................... 23 Abstracts of Talks ........................................... 24 Posters ........................................................... 44 Index of Authors ........................................... 111 Directory of Participants ................................ 121

GENERAL INFORMATION

PROGRAM. The short abstracts for the talks and posters appear in this book and are arranged in the order of presentation. The author index references the program code of presentations. CONFERENCE CD includes long abstracts of all presentations. POSTERS are divided into two spaces. • Posters 001-306 are in the Atrium • Posters 307 - 412 are in Chopin Ballroom POSTER SET UP should be complete by 9:00 am on Monday. Please remove posters at 3:45 pm on Thursday. Note: Place posters in the space number printed in this program. See page 44. • Monday, 2:00 – 3:45 pm: Authors of posters in odd

numbered spaces (001, 003, 005, etc) present. • Tuesday, 2:00 – 3:45 pm: Authors of posters in even

numbered spaces (002, 004, 006 etc) present. • Wednesday, 2:00 – 3:45 pm: Authors of posters in odd

numbered spaces (001, 003, 005, etc) present. • Thursday, 2:00 – 3:35 pm: Authors of posters in even

numbered spaces (002, 004, 006 etc) present. TALKS. Plenary session talks are in the Versailles Ballroom. Parallel session talks are scheduled in either Versailles Ballroom or Trianon Ballroom as indicated in the program.

Speakers must arrive ½ hour prior to the start of their sessions. Speakers will use this time to connect laptops and assure compatibility with the projector. MESSAGES. Message boards near conference registration on level two. INTERNET ACCESS. WiFi is provided in the Atrium and Ballroom areas. • Select wireless network

INTERCONTINENTAL_MEETING_ROOMS • Password is enc2012 Guest rooms in the Intercontinental Hotel have free Internet. HOSPITALITY SUITES and EXHIBIT BOOTHS. Vendor hospitality suites are located in the hotel. Exhibit booths are in the Ballroom Foyer. Refer to pages 9-10 for locations. Have a label applied to your raffle card from each vendor and return to ENC conference registration by 12 noon on Thursday to enter raffle on Thursday evening. You must be present to win. SPECIAL EVENTS Sunday, 6:30 – 8:00 pm Viva ENC! Poolside. All registrants are invited to a festive

Cuban style reception. No extra ticket is required, only your ENC name badge (any color). Please present the drink ticket in your registration envelope for one Mojito - Olé!

Thursday, 6:30 - 8:00 pm Conference Banquet, Chopin Ballroom. Please present

your ticket to server. Tickets may be purchased until 12 noon on Monday. Cost is $50.

Thursday, 8:00 – 9:00 pm After Dinner Program, Versailles Ballroom

Richard R. Ernst ENC: A Major Stimulator in My Scientific Life

Vendor Raffle: Turn in completed form by 12 noon on Thursday to enter. You must be present at the After Dinner Program to win.

EMPLOYMENT CENTER. Poster boards in the Conference registration area are provided for employment notices. If you are seeking employment, please supply at least 20 copies of your résumé to conference registration after 10:00 am on Monday. The résumés will be filed for public perusal.

2013 GÜNTHER LAUKIEN PRIZE: CALL FOR NOMINATIONS

The nominated work should be published within the last three years. In some special cases, the award may be for cumulative achievements over a longer period. Nominations should include the following and be submitted by October 31: 1. Name of nominee, the nominee’s affiliation, address,

phone, fax and e-mail. 2. Name of nominator, address, phone, fax and e-mail. 3. A brief (no more than 200 words) description of the work

serving as the basis for the nomination. 4. A list of relevant publications (no more than 5). Email to: [email protected]) REGULATIONS • Name badges are required for all conference sessions,

including the posters. A white (full registration) badge is required for oral and poster sessions.

• NO SMOKING is permitted in any conference area. • Cell phones must be turned off in oral sessions. • NO photography or recording is permitted in any

session, including posters. • There may be no organized activities (even off-site)

other than those approved by ENC during the conference week (5:00 pm on Sunday through noon on Friday).

GÜNTHER LAUKIEN PRIZE 2012

Klaes Golman

Jan Henrik Ardenkjaer-Larsen

The Günther Laukien Prize 2012 is awarded to Klaes Golman and Jan Henrik Ardenkjaer-Larsen for the conception, development, and application of dissolution-DNP NMR.This remarkable technique is capable of enhancing the nuclear polarization by several orders of magnitude. It provides access to a panacea for new spectacular applications that were so far inconceivable because of lacking signal strength. The method starts with Dynamic Nuclear Polarization (DNP) of the solidified sample at very low temperature in the presence of a radical, such as trityl, by microwave irradiation. Up to 65% 13C polarization can be achieved. Through a highly efficient dissolution process by injecting a hot solvent, the polarized sample is rapidly brought into solution at room temperature and is ready to be applied to a variety of situations where high-sensitivity, high-resolution liquid-state NMR is indispensable. A surprising polarization gain of up to four orders of magnitude can be achieved in solution at ambient temperature. The most promising applications of dissolution-DNP have been found in the medical field where numerous situations require indeed several orders of magnitude more nuclear polarization. Especially the studies of low-concentration metabolites can profit enormously from the advent of dissolution-DNP. While before most biomedical studies were confined to high-sensitivity proton magnetic resonance, carbon-13 resonance with its numerous advantages regarding specificity becomes now feasible as well. For example, observing hyperpolarized 13C-labeled bicarbonate allows for in-vivo pH measurements, and studying the 13C-pyruvate metabolism permits in-vivo tumour diagnosis. In the same sense, solving analytical problems in chemistry and molecular biology often demands higher signal strength than available in the past. The technique shows unusual features that need to be taken into account when optimizing the usage of dissolution-DNP. The time necessary for achieving a high degree of polarization by DNP can be in the order of minutes to hours. And the polarization is available only for a short time period in the order of a typical T1-relaxation time. A second high-field magnet is needed for the low-temperature pre-polarization of the solidified solute, besides the spectroscopy or imaging magnet. The instrumental set-up can therefore be quite demanding. • Klaes Golman is Professor em. in Experimental Diagnostic Radiology, formerly with the University of Lund, Sweden. He is

presently CEO of Imagnia AB, Malmö, Sweden. • Jan Henrik Ardenkjaer-Larsen is Adjoint Professor at the Technical University of Denmark, Department of Electrical

Engineering. He is associated with General Electric Healthcare, Brondby, Denmark. During the eight years since the conception of dissolution-DNP, Golman, Ardenkjaer, and their research teams have demonstrated spectacular applications in numerous publications, of which only some representative ones are listed here:

1. J.H. Ardenkjaer-Larsen, B. Fridlund, A. Gram, G. Hansson, L. Hansson, M.H. Lerche, R. Servin, M. Thaning, and K. Golman, Proc. Natl. Acad. Sci. USA 100, 10158-10163; “Increase in signal-to-noise ratio of >10’000 times in liquid-state NMR”.

2. K. Golman, J.H. Ardenkjaer-Larsen, J.S. Peterson, S. Mansson, and I. Leunbach, Proc. Natl. Acad. Sci. USA 100, 10435-10439; “Molecular imaging with endogenous substances”.

3. K. Golman, L.E. Olsson, O. Axelsson, S. Mansson, M. Karlsson, and J.S. Petersson, Brit. J. Radiology 76, 8118-8127 (2003); “Molecular imaging using hyperpolarized 13C”.

4. K. Golman, R. in‘t Zandt, M. Thaning, Proc. Natl. Acad. Sci. USA 103, 11270-11275 (2006); “Real-time metabolic imaging”. 5. K. Golman, R. in’t Zandt, M. Lerche, R. Pehrson, and J.H. Ardenkjaer-Larsen, Cancer Res. 66, 10855-10860 (2006): “Metabolic

imaging by hyperpolarized 13C magnetic resonance imaging for in vivo tumor diagnosis”. 6. S.E. Day, M.I. Kettunen, F.A. Gallagher, D.-E. Hu, M. Lerche, J. Wolber, K. Golman, J.H. Ardenkjaer-Larsen, and K.M. Brindle, Nature

Med. 13, 1382-1387 (2007); “Detecting tumor response to treatment using hyperpolarized 13C magnetic resonance imaging and spectroscopy”.

7. F.A. Gallagher, M.I. Kettunen, S.A. Day, D.-E. Hu, J.H. Ardenkjaer-Larsen, R. in’t Zandt, P.R. Jensen, M. Karlsson, K. Golman, M.H. Lerche, and K.M. Brindle, Nature 453, 940-944 (2008); “Magnetic resonance imaging of pH in vivo using hyperpolarized 13C-labelled bicarbonate”.

8. H. Jóhannesson, S. Macholl, and J.H. Ardenkjaer-Larsen, J.Magn.Reson. 197, 167-175 (2009); “Dynamic nuclear polarization of [1-13C]pyruvic acid at 4.6 tesla”.

9. J.H. Ardenkjaer-Larsen, A.M. Leach, N. Clarke, J. Urbahn, D. Anderson, and T.W. Skloss, NMR Biomed. 24, 927-932 (2011); “Dynamic nuclear polarization polarizer for sterile use intent”.

RITCHEY TRAVEL AWARD 2012

The ENC Ritchey Travel Award is established to honor William M. Ritchey, who is Professor Emeritus of Chemistry and Macromolecular Science at Case Western Reserve University. William Ritchey founded the ENC in 1960. The award is fully funded with contributions from Professor Ritchey’s former students. The areas of the Award are to reflect Prof. Ritchey’s broad interests in the development and application of NMR to chemical and material sciences. The 2012 recipient of the ENC Ritchey Travel Award is Ms. Ishita Sengupta. Ishita is a fifth year graduate student working in the laboratory of Christopher P. Jaroniec at the Ohio State University. Ishita’s research focuses on the development of new solid-state NMR methods for rapid determination of protein

structures by exploiting the electron-nucleus hyperfine couplings, from which long-range distance restraints can be obtained site-specifically through the measurements of the distance-dependent paramagnetic relaxation enhancements. Ishita’s Ritchey’s Award winning work demonstrates that multiple 15N PRE restraints can be measured in a protein and, together with chemical shift and torsion angle restraints, used to derive the 3D protein fold. In addition to her research accomplishments, Ishita is a mentor of undergraduate and graduate students in the Jaroniec laboratory. Ishita’s long-term goal is to obtain an academic position where she can uncover her research and teaching talents to the fullest extent.

SURAJ P. MANRAO SCIENCE FUND Student Travel Recipients funded by Suraj Manrao Science Foundation

ENC is pleased to acknowledge the continuation of support from the Suraj P. Manrao Student Travel Fund. During his long career, Mr. Manrao has been dedicated to the NMR community and has a special interest in helping and guiding young scientists in the beginning of their careers. This fund represents his commitment to this community and an investment in the future of young post-doctoral fellows and graduate students.

Emeline Barbet-Massin

CRMN / ENS Lyon Mark Bostock

University of Cambridge Julia Gath

ETH Zuerich Andree Gravel

University of Quebec Lukasz Jaremko

University of Warsaw Pavel Kaderavek Masaryk University

Yang Li University of Wyoming

Luciana Elena Machado Federal University of Rio de Janeiro

Veera Mohan Rao Indian Institute of Chemical Technology

Wazo Z. Myint University of Pittsburgh

Berit Paaske Aarhus University

G Jithender Reddy Tata Institute of Fundamental Research

Emily Ritz University of Guelph

Matsyendra Nath Shukla IISER Mohali

Kanchan Sonkar Ctr of Biomedical Magnetic Resonance

Suhas Tikole University of Frankfurt

Ilker Un Gebze Institute of Technology

Jayasubba Reddy Yarava Indian Inst of Science

Weihua Ye Stockholm University

Liu Zhu Wuhan Institute of Physics and Math.

Siqi Zhu McGill University

STUDENT TRAVEL STIPENDS

Funds provided by ENC and these donors

Cambridge Isotope Laboratories

Wilmad / Lab Glass

Bridge 12 Technologies Inc. Doty Scientific, Inc. Revolution NMR LLC Tecmag

Student Travel Recipients funded by the sponsors above Loren Andreas

MIT Andreea Cristina Balaceanu

Functional and Interactive Polymers David Ban Max Planck Bao Qingjia

Huazhong Univ of Sci & Tech Ryan Davis

Duke University Stephen DeVience Harvard University Matthew T. Eddy

MIT El Mohammed Halidi

CNRS Stefan Henning

TU Dortmund Yonatan Hovav

Weizmann Inst of Science Carson Ingo

Univ of Illinois at Chicago Mariusz Jaremko

Univ of Warsaw Fangling Ji

University of Pittsburgh Louis Jones

UC Santa Barbara

Huseyin Kara University of Pennsylvania

Monica Kinde-Carson Univ of Nebraska-Lincoln

Derek Langeslay UC Riverside

Regan LeBlanc University of Maryland

Hongde Li Wuhan Inst of Physics & Math

Zhao Li UCLA

Ting Liu Clark University

Jiaoshi Lu UC San Diego Bryan Lucier

University of Windsor Wenping Mao

Natl High Magnetic Field Lab, FSU Hussain Masoom

University of Toronto Erick Meneses Ramirez

McGill University Krystal A. Morales

Texas A&M University Kaustubh Mote

Univ of Minnesota

Kristin Nuzzio University of Illinois

Ann-Christin Poppler Georg August Universitat Alexandra Pozhidaeva UCONN Health Center Mukundan Ragavan Texas A&M University

Nicola Salvi Ecole Polytechnique

Christopher Schmidt Univ of South Carolina

Lisa Vingara Oregon Health & Science Univ

Laura Walkup Southern Illinois University

Tuo Wang Iowa State Univeristy

LI Xie Michigan State University

Xiang Xu New York University

Yanli Zhang University of Nebraska

Zhiyang Zhang Virginia Polytechnic Institute

Xiaowei Zou Columbia University

ENC acknowledges the work of Tatyana Polenova who coordinated the Travel Stipends.

Anatole Abragam

Dec. 1914 – June 8, 2011

Albert Overhauser

Aug. 17, 1925 – Dec 10, 2011

Paul T. Callaghan

Aug. 19, 1947 – March 24, 2012

IN MEMORIAM

Since the last ENC, three giants in the field of NMR have passed away. Here we gratefully acknowledge their prolific careers and brilliant personalities. They will be sorely missed.

Born in Russia, Abragram emigrated to France in 1925 where he was educated at the University of Paris and served in World War II. He earned his Ph.D. in 1950 from Oxford University, supervised by Maurice Pryce. In 1955 he founded the Laboratory of Magnetic Resonance at Saclay and continued as its director for 30 years. His many achievements include: formalisms of nuclear relaxation, development of the concept of spin temperature, muon spectroscopy, pseudo-magnetic resonance of neutron spins, and early contributions to earth-field magnetometry and dynamic nuclear polarization. To younger generations, Abragam is perhaps best known for his elegant and erudite “Principles of Nuclear Magnetism”, a monograph first published in 1961 that has been foundational for the education of countless spectroscopists, and his autobiography “Time Reversal”. Abragam was an Honorary Fellow of Merton, Magdalen and Jesus Colleges at Oxford University, a Foreign Honorary Member of the American Academic of Arts and Sciences, and recipient of the Lorentz Medal in 1982.

Overhauser was born in San Diego and went on to the University of California at Berkeley where he earned B.A. (1948) and Ph.D. (1951) degrees, after having his studies interrupted to serve in the U.S. Navy in World War II. He spent portions of his early career at the University of Illinois, Cornell University and Ford Motor Company, and then settled at Purdue University for the final 30 years of his career as the Stuart Distinguished Professor of Physics. Overhauser’s name is synonymous with one of the most important concepts in NMR, and the effect forms the basis for studies ranging from dynamic nuclear polarization of surfaces to structure determination of proteins. For these and other seminal contributions, he was awarded the National Medal of Science by President Clinton in 1994. He was also a member of the National Academy of Science, the American Academy of Arts and Sciences, and recipient of the Oliver E. Buckley and Russell Varian Prizes.

Callaghan was a brilliant scientist and passionate advocate for investment in fundamental science, dissemination of its wonder to broad audiences, and commercialization of its applications. He was educated at Victoria University of Wellington and Oxford, after which he returned to New Zealand in 1974. He was an outstanding lecturer, in particular for general audiences, and reached out to the public through radio series and books such as “As Far as We Know: Conversations about Science, Life and the Universe”. He also wrote a cornerstone text, “Principles of Nuclear Magnetic Resonance Microscopy”, in 1994. He was founding director of Magritek, which develops NMR and MRI products emphasizing portability, unique applications for industry, and laboratory education. Among his numerous awards, Callaghan was the sole recipient of ENC’s Günther Laukien Prize in 2010 “for his seminal contributions to the study of polymeric and heterogeneous materials by advanced NMR exchange, diffusion and relaxation techniques… and innovative q-space-diffusion-related developments”.

CORPORATE SPONSORS

ENC is pleased to acknowledge the generous support of the following companies.

Major Sponsors

Sponsor

Doty Scientific, Inc. Isotec

JS Research, Inc. Magritek Limited

MEDIA PARTNERS

ENC is pleased to acknowledge the advertising support of these Publishers and Journals.

Elsevier Springer Wiley

Journal of Magnetic Resonance

Journal of Biomolecular NMR

Magnetic Resonance in

Chemistry

Progress in Nuclear Magnetic Resonance Spectroscopy

NMR in Biomedicine

Solid State Nuclear Magnetic Resonance

HOSPITALITY SUITES AND EXHIBIT BOOTHS

Hospitality Suites Exhibit Booths Sunday After 8:00 pm (optional)

Monday - Wednesday After 6:00 pm 10:15 - 10:45 am 2:00 - 3:45 pm

Thursday After 6:00 pm (optional) 10:15 - 10:45 am 2:00 - 3:45 pm

Be sure to enter the raffle by asking exhibitors to apply labels to your card at each suite and exhibit booth. Completed cards must be returned to conference registration by noon on Thursday. The drawing will take place Thursday evening during the after dinner program in Versailles Ballroom. You must be present to win. Exhibit booths are located in the Ballroom Foyer on the second level just outside the session rooms. Hospitality suites are located on the lobby level. Company Location

ACD/Labs Marti ACT GmbH Crandon

AGILENT TECHNOLOGIES Bayfront B BRUKER Bayfront A

CAMBRIDGE ISOTOPE LABS Flagler CPC Booth 3

DAEDALUS INNOVATIONS LLC Booth 10 DOTY SCIENTIFIC Gusman

ELSEVIER SCIENCE LTD. Tabletop Display FTS SYSTEMS/SP SCIENTIFIC Booth 9

ISOTEC Isles JEOL USA, INC. Sevilla

JS RESEARCH, INC. Booth 2 MAGNETICS BUSINESS & TECHNOLOGY Tabletop Display

MAGRITEK LIMITED Crandon MESTRELAB RESEARCH Deering

MR RESOURCES, INC. Booths 6-7 NEW ERA ENTERPRISES Booth 11

NMR ASSOCIATES Dupont NORELL, INC. Trade Room

OPEN TECHNOLOGIES, INC. Dupont OPTIGRATE CORP. Booth 1

PICOSPIN, LLC Booth 5 RESONANCE CONSULTING LLC Dupont

REVOLUTION NMR LLC Board Room SHIGEMI, INC. Godfrey

SPRINGER-VERLAG NEW YORK Tabletop Display STELAR s.r.l Booth 8

TECMAG Booth 4 TRIANGLE ANALYTICAL, INC. Godfrey

WILEY-BLACKWELL Tabletop Display WILMAD/LAB GLASS Tuttle

INTERCONTINENTAL HOTEL

Lobby Level

Level Two

Shigemi / Triangle ACT / Magritek Revolution NMR Mestrelab ACD/Labs Doty Wilmad/Lab Glass

NMR Associates Open Technologies Resonance Consulting

Cambridge Isotope Labs

Norell Inc. Bruker Agilent JEOL

Isotec

Exhibit Booths CPC Daedalus Innovations FTS Systems/SP Scientific JS Research MR Resources New Era Enterprises Optigrate Corp. Picospin Stelar Tecmag

POSTERS Atrium Foyer Chopin Ballroom

Session / Plenary Room Versailles Ballroom

Session Room Trianon Ballroom

53rd ENC PROGRAM OVERVIEW

SUNDAY April 15

3:00-9:00 pm, Registration 6:30-8:00 pm, Welcome Reception, Poolside (weather permitting)

8:00-11:30 pm, Hospitality Suites (Optional) MONDAY April 16

9:00-10:15 am, Plenary Session: Welcome & Laukien Prize Lecture, Versailles Ballroom 10:15-10:45 am, Break

10:45 am -12:30 pm, (MOB) Plenary Session: Biomolecules Structure and Function, Versailles Ballroom

12:30-2:00 pm, Lunch Break 2:00-3:45 pm, Poster Session. Authors of odd-numbered posters present.

4:00-6:00 pm, (MOD) Solids I, Versailles Ballroom

4:00-6:00 pm, (MOE) Detection,Trianon Ballroom

7:00-9:00 pm, AMMRL Meeting, Trianon After 6:00 pm, Hospitality Suites

TUESDAY April 17

8:30-10:15 am, (TOA) Plenary Session: Biomolecular NMR, Versailles Ballroom 10:15-10:45 am, Break

10:45 am-1:00 pm, (TOB) Tutorial Session, Versailles Ballroom

10:45 am-12;30 pm, (TOC) Materials, Trianon Ballroom

12:30-2:00 pm, Lunch Break 2:00-3:45 pm, Poster Session. Authors of even-numbered posters present.

4:00-6:00 pm, (TOD) Dynamics, Versailles Ballroom

4:00-6:00 pm, (TOE) MRI Developments,Trianon Ballroom

After 6:00 pm, Hospitality Suites WEDNESDAY April 18

8:30-10:15 am, (WOA) Plenary Session, Resolution and Sensitivity, Versailles Ballroom 10:15-10:45 am, Break

10:45 am-12:30 pm, (WOB) Small Molecules, Versailles Ballroom

10:45 am-12:30 pm, (WOC) Exotica, Trianon Ballroom

12:30-2:00 pm, Lunch Break 2:00-3:45 pm, Poster Session. Authors of odd-numbered posters present.

4:00-6:00 pm, (WOD) Motion and Dynamics, Versailles Ballroom

4:00-6:00 pm, (WOE) MRI / MRS, Trianon Ballroom

After 6:00 pm, Hospitality Suites THURSDAY April 19

8:30-10:15 am, Plenary Session: (ThOA) Exotica MRI, Versailles Ballroom

10:15-10:45 am, Break 10:45 am-12:30 pm, (ThOB) Screening,

Versailles Ballroom 10:45 am-12:30 pm, (ThOC) Solids II,

Trianon Ballroom 12:30-2:00 pm, Lunch Break

2:00-3:45 pm, Poster Session. Authors of even-numbered posters present. 4:00-6:00 pm, (ThOD) Software and

Hardware, Versailles Ballroom 4:00-6:00 pm, (ThOE) ENC Focus: NMR in Latin & South America, Trianon Ballroom

After 6:00 pm, Hospitality Suites (Optional) 6:30-8:00 pm, Conference Dinner, Chopin Ballroom. Ticket required

8:00-9:00 pm, After Dinner Program, Versailles Ballroom Raffle. Completed cards must be turned into conference registration. Must be present to win.

FRIDAY April 20

8:30-10:15 am, Plenary Session: Frontiers, Versailles Ballroom 10:15-10:45 am, Break

10:45-12:30 pm, Plenary Session: Large Systems, Versailles Ballroom

SUNDAY, APRIL 15

6:30 –8:00 pm WELCOME RECEPTION for all conferees

Pool Terrace

After 8:00 pm HOSPITALITY SUITES OPEN (optional)

MONDAY, APRIL 16

All posters should be set up 8:00 – 9:00 am. Posters 001 - 306 are in the atrium. Posters 307 - 412 are in Chopin Ballroom. Be sure to use the poster space numbers with the abstracts in this program. See page 44.

9:00 – 10:15 am, MONDAY MORNING

OPENING SESSION, A. J. Shaka, presiding Versailles Ballroom

9:00-9:05 Welcome; A. J. Shaka, Chair, 53rd ENC

9:05-9:20 Presentation of the 2012 Günther Laukien Prize; Richard R. Ernst

9:20-10:15 Laukien Prize Lecture Hyperpolarization by Dissolution-DNP:

History, Development and Applications Jan Henrik Ardenkjaer-Larsen Klaes Golman

Frank Laukien, a sponsor of the Laukien Prize, and Richard Ernst, Chair of the Laukien Prize Committee

10:15 – 10:45 am, BREAK

10:45 am – 12:20 pm, MONDAY MORNING

BIOMOLECULES STRUCTURE AND FUNCTION A. J. Shaka, presiding

Versailles Ballroom Abstract Page MOB 10:45-11:10 Proteins in Flagrante; Dorothee Kern; Brandeis University, Boston, MA

MOB 11:10-11:35 The Dynamic Structure of a Viral Fusion Domain and its Interaction with Lipids from RDCs and Size-Dispersed Relaxation; Justin Lorieau; John Louis; Ad Bax; NIH, Bethesda, MD ...................... 24

MOB 11:35-11:50 Atomic Resolution Dynamics on the Surface of Amyloid beta Protofibrils Probed by Dark State Exchange Saturation Transfer (DEST) spectroscopy; Nicolas Fawzi1; Jinfa Ying1; Rodolfo Guirlando1; Dennis Torchia2; Marius Clore1; 1NIDDK, NIH, Bethesda, MD; 2NIDCR, NIH, Bethesda, MD .............................................................................................................................................. 24

MOB 11:50-12:05 Structure and Dynamics of a Microcrystalline Metalloprotein by Solid-state NMR : Proton-detection, Ultra-fast MAS and Paramagnetic Restraints; Michael J. Knight1; Andrew Pell1; Ivano Bertini2; Isabella C. Felli2; Leonardo Gonnelli2; Roberta Pierattelli2; Torsten Herrmann1; Lyndon Emsley1; Guido Pintacuda1; 1ENS-Lyon, Villeurbanne, France; 2CERM - University of Florence, Florence, Italy (also poster 390) .................................................................................................. 24

MOB 12:05-12:20 Characterizing the Role of VDAC1's N-Terminus in Channel Gating with Magic Angle Spinning NMR; Matthew T. Eddy1; Oscar Hermida2; Lindsay Clark1; Loren Andreas1; Yongchao Su1; Patrick van der Wel1; Gerhard Wagner3; Tatiana Rostovtseva2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA; 2National Institutes of Health, Bethesda, MD; 3Harvard Medical School, Boston, MA ................................................................................ 24

12:30 – 2:00 pm, LUNCH BREAK

MONDAY, APRIL !6, continued

2:00 – 3:45 pm POSTER SESSION

Abstracts begin on page 46. Authors of odd numbered spaces (001, 003, 005, etc) present. Posters 001 - 306, Atrium. Posters 307 - 412, Chopin Ballroom

4:00 – 5:50 pm, MONDAY AFTERNOON

SOLIDS I Philip Grandinetti, presiding

Versailles Ballroom Abstract Page MOD 4:00-4:25 NMR Crystallography in the Enzyme Active Site of Tryptophan Synthase; Leonard J Mueller;

University of California, Riverside, CA ......................................................................................................... 25

MOD 4:25-4:50 SSNMR Investigations of Proton Conduction and Membrane Curvature Generation by an Ion Channel; Mei Hong; Iowa State, Ames, IA ................................................................................................. 25

MOD 4:50-5:05 MAS NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A; Loren Andreas1; Matthew T. Eddy1; James Chou2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA; 2Harvard Medical School, Boston, MA ................................................................................................. 25

MOD 5:05-5:20 S-RESPDOR for Inter-Nuclear Distance Measurement between Spin-1/2 and Quadrupolar Nuclei; Jean Paul Amoureux; Xingyu LU; Olivier Lafon; Frederique Pourpoint; Lille university, Villeneuve D'ascq, France ........................................................................................................................... 25

MOD 5:20-5:35 Protein Fold Determined by Paramagnetic Magic-Angle Spinning Solid-State NMR Spectroscopy; Ishita Sengupta; Graduate Student, Columbus, OH (also poster 391) .............................. 25

MOD 5:35-5:50 Developing a Fully Broadband Cross-Polarization Experiment using Adiabatic Pulses: Theory and Experiment for the BRAIN-CP Pulse Sequence; Robert W. Schurko1; Kristopher J. Harris1; Bryan E.G. Lucier1; Adonis Lupulescu2; Lucio Frydman2; 1University of Windsor, Windsor, Canada; 2Weizmann Institute, Rehovot, Israel ........................................................................................................... 25

4:00 – 5:50 pm, MONDAY AFTERNOON

DETECTION James Prestegard, presiding

Trianon Ballroom Abstract Page MOE 4:00-4:25 Detection of Spin Polarization in Semiconductors with Optical-Pumping; Dustin Wheeler1; Erika

Sesti1; Wieland Worthoff2; Christopher Stanton3; Sophia E. Hayes1; 1Washington University, Saint Louis, MO; 2TU Dortmund, Dortmund, Germany; 3University of Florida, Gainesville, FL ............................ 26

MOE 4:25-4:50 Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy; Anne Lesage; University of Lyon, High Field NMR Center, Villeurbanne, France ............................................................................... 26

MOE 4:50-5:05 Near-Field Microprobes : NMR and MRI Applications; El Mohamed Halidi1; Eric Nativel2; Laurent Mahieu-Willame3; Paul C. Stein4; Nadia Bertin5; Rémy Schimpf6; Michel Zanca1; Christophe Goze-BAC1; 1NanoNMRI UM2-CNRS L2C UMR5221, Montpellier, France; 2UM2-CNRS IES UMR5214, Montpellier, France; 3CNRS CREATIS UMR5220, Lyon, France; 4FKF-SDU, Campusvej, Odense, Denmark; 5PHS INRA, Avignon, France; 6RS2D, Bischwiller, France ......................................................... 26

MOE 5:05-5:20 Design Considerations for High-Temperature-Superconducting NMR Probes; Vijaykumar Ramaswamy1; Jerris Hooker2; Richard Withers3; Robert Nast3; William Brey2; Arthur Edison1, 2; 1University of Florida, Gainesville, FL; 2National High Magnetic Field Lab, Tallahassee, FL; 3Agilent Technologies, Santa Clara, CA (also poster 392) ....................................................................................... 26

MOE 5:20-5:35 PHIP Monitoring of Conformational Changes and Stereoselective Reactions; Xiang Xu1; Boyang Zhang1; Joel A Tang1, 2; Francesca Gruppi1; James Canary1; Alexej Jerschow1; 1New York University, New York, NY; 2NHMFL FSU, Tallahassee, FL .......................................................................................... 26

MOE 5:35-5:50 First Microfabricated Inserts for Magic Angle Coil Spinning (MACS) NMR Spectroscopy; Vlad Badilita; University of Freiburg, Freiburg Im Breisgau, Germany ................................................................. 26

After 6:00 pm, HOSPITALITY SUITES OPEN

7:00 – 9:00 pm, AMMRL (Association of Managers of Magnetic Resonance Laboratories), Trianon Ballroom

TUESDAY, APRIL 17

8:30 – 10:05 am, TUESDAY MORNING BIOMOLECULAR NMR

Teresa Carlomagno, presiding Versailles Ballroom

Abstract Page TOA 8:30-8:55 NMR Detection of Structures in the HIV-1 5′-Leader RNA: Insights into the Mechanism of HIV-1

Genome Packaging; Xiao Heng; UMBC, Baltimore, MD ........................................................................... 27

TOA 8:55-9:20 Function of the Shwachman-Bodian-Diamond syndrome Protein in Ribosome Assembly; Christine Hilcenko; MRC, Cambridge, United Kingdom .............................................................................. 27

TOA 9:20-9:35 High Resolution Structure of a Large Membrane Protein by Joint X-ray/NMR Calculations and Paramagnetic Relaxation Sensitivity Enhancement; Ming Tang1; Deborah Berthold1; Lindsay J Sperling1; Charles Schwieters2; Anna Nesbitt1; Andrew J. Nieuwkoop1; Robert Gennis1; Chad Rienstra1; 1University of Illinois at Urbana-Champaign, Urbana, IL; 2National Institutes of Health, Bethesda, MD .............................................................................................................................................. 27

TOA 9:35-9:50 Compressed Sensing Reconstruction of Undersampled NOESY Spectra: Application to Large Membrane Proteins; Mark Bostock1; Daniel Holland2; Daniel Nietlispach1; 1Department of Biochemistry, University of Cambridge, United Kingdom; 2Magnetic Resonance Research Centre, University of Cambridge, United Kingdom (also poster 393) ....................................................................... 27

TOA 9:50-10:05 NMR Detection of Redox Reactions in Cu2+-Bound Amyloid-β Fibrils and Resolution Enhanced Solid-State NMR by SAIL and Ultra Fast MAS; Sudhakar Parthasarathy1; Yusuke Nishiyama2; Yuki Endo2; Takahiro Nemoto2; Masatsune Kainosho3, 4; Yoshitaka Ishii1; 1Univ. of Illinois at chicago, Chicago, IL; 2JEOL Ltd., Tokyo, Japan; 3Graduate School of Science, Nagoya University, Nagoya, Japan; 4Center of Priority Areas, Tokyo Metropolitan Univ, Tokyo, Japan (also poster 394) ...................... 27

10:15 – 10:45 am BREAK

TUESDAY, APRIL 17, continued

10:45 am – 1:00 pm, TUESDAY MORNING TUTORIAL SESSION Sangi Han, presiding Versailles Ballroom

Abstract Page TOB 10:45-11:20 ABC's of NUS; Jeffrey C. Hoch; Univ of Connecticut Health Ctr, Farmington, CT ..................................... 28

TOB 11:20-12:25 Design, Care and Feeding of NMR Probes: A Tutorial Part II; Kurt Zilm; Yale University, New Haven, CT ................................................................................................................................................... 28

TOB 12:25-1:00 Ultrafast Multidimensional NMR – A Coherent Picture?; Lucio Frydman; Weizmann Institute, Rehovot, Israel ............................................................................................................................................ 28

10:45 am – 12:20 pm, TUESDAY MORNING

MATERIALS Lyndon Emsley, presiding

Trianon Ballroom Abstract Page TOC 10:45-11:10 The Benefits and Curses of Ultrabroad NMR Signals: Methodological Advancements and

Scientific Insights from Solid-State 195Pt NMR; Brad Chmelka; University of California, Santa Barbara, Santa Barbara, CA ........................................................................................................................ 29

TOC 11:10-11:35 Insights into Radiation Damage and Nuclear Materials from High-Resolution Radiological Nuclear Magnetic Resonance; Ian Farnan; University of Cambridge, Cambridge, United Kingdom ........ 29

TOC 11:35-11:50 High Resolution Stray Field Imaging Probe for In Situ Battery Studies; Joel A Tang1; Guiming Zhong2; Jason Kitchen1; Peter L. Gor'kov1; Riqiang Fu1; 1National High Magnetic Field Laboratory, Tallahassee, FL; 2Xiamen Univeristy, Xiamen, PR China ........................................................................... 29

TOC 11:50-12:05 Ion Clustering and Transport in Organic Electrolytes: New Insights from PFG NMR; Jianbo Hou; Zhiyang Zhang; Mark D Lingwood; Bryce E Kidd; Louis A Madsen; Virginia Tech, Blacksburg, VA ............................................................................................................................................................... 29

TOC 12:05-12:20 A Large Sample Volume Magic Angle Spinning Nuclear Magnetic Resonance Probe for In-Situ Investigations with Constant Flow of Reactants; Jian Zhi Hu; Jesse A Sears; Hardeep Mehta; Joseph Ford; Ja Hun Kwak; Kake Zhu; Yong Wang; Jun Liu; David W Hoyt; Mary Hu; Ju Feng; Charles H. F. Peden; Pacific Northwest National Laboratory, Richland, WA............................................... 29

12:30 – 2:00 pm LUNCH BREAK


Abstracts begin on page 44. Authors of even numbered spaces (002, 004, etc) present. Posters 001 - 306, Atrium. Posters 307 - 412, Chopin Ballroom

TUESDAY, APRIL 17, continued

4:00 – 5:50 pm, TUESDAY AFTERNOON DYNAMICS

Rafael Bruschweiler, presiding Versailles Ballroom

Abstract Page TOD 4:00-4:25 Ligand Binding and Helix Interactions in GPCR Activation; Steven Smith; Stony Brook University,

Stony Brook, NY .......................................................................................................................................... 30

TOD 4:25-4:50 NMR and Molecular Dynamics Simulations: A Perfect Match?; Kresten Lindorff-Larsen; Department of Biology, University of Copenhagen, Copenhagen, Denmark ............................................... 30

TOD 4:50-5:05 Analysis Pipeline for Simultaneous Study of Structure and Dynamics of Challenging Proteins from Residual Dipolar Couplings; Stephanie Irausquin; Christopher Schmidt; Mikhail Simin; Homayoun Valafar; University of South Carolina, Columbia, SC (also poster 395) ..................................... 30

TOD 5:05-5:20 Dynamics of the Equine Infectious Anemia Virus Capsid Protein: Structural and Functional Implications for the Conserved β-Hairpin; Kang Chen1; Grzegorz Piszczek1; Carol Carter2; Nico Tjandra1; 1National Institutes of Health, Bethesda, MD; 2State University of New York Stony Brook, Stony Brook, NY .......................................................................................................................................... 30

TOD 5:20-5:35 Model of Large Scale Conformation Mobility in Proteins; Yaroslav Ryabov1; G. Marius Clore2; Charles D. Schwieters1; 1DCB, CIT, NIH, Bethesda, MD; 2NIDDK, NIH, Bethesda, MD (also poster 396) ............................................................................................................................................................. 30

TOD 5:35-5:50 Expanding Limits of Relaxation Dispersion: Combined Bayesian CPMG, R1rho, and Lineshape Analysis of Low-Populated, Fast-Exchanging Protein States; Lukas Zidek1; Petr Padrta1; Pavel Kaderavek1; Mikael Akke2; Carl Diehl2; Hana Sanderova3; Veronika Papouskova1; Libor Krasny3; Vladimir Sklenar1; 1Masaryk University, Brno, Czech Republic; 2Lund University, Lund, Sweden; 3Academy of Sciences of the Czech Republic, Prague, Czech Republic ..................................... 30

4:00 – 5:50 pm, TUESDAY AFTERNOON

MRI DEVELOPMENTS Michael Garwood, presiding

Trianon Ballroom Abstract Page TOE 4:00-4:25 New Concepts for Spatial Encoding; Jürgen Hennig; University Hospital Freiburg, Freiburg,

Germany ...................................................................................................................................................... 31

TOE 4:25-4:50 Maximum Multiplexing and Parallelization for Encoding with Detectors in MRI; Larry Wald; MGH NMR Core at Martinos Center, Charlestown, MA .............................................................................. 31

TOE 4:50-5:05 Tracking Dopamine-induced Manganese Transport in the Nervous System of Aplysia californica with MEMRI; Ileana Jelescu1; Romuald Nargeot2; Denis Le Bihan1; Luisa Ciobanu1; 1CEA/DSV/I2BM/Neurospin, Paris, France; 2Université Bordeaux, Bordeaux, France ................................ 31

TOE 5:05-5:20 Modifying Doxorubicin Nano-carriers to Create CEST MRI Contrast and Subsequent Use for Monitoring Cervical Tumor Therapy; Kannie Chan2; Tao Yu2; Guanshu Liu1; Ming Yang2; Assaf Gilad2; Peter Van Zijl2; Jeff Bulte3; Justin Hanes2; Michael T. Mcmahon1; 1Johns Hopkins University SOM/KKI, Baltimore, MD; 2Johns Hopkins University School of Medicine, Baltimore, MD; 3Johns Hopkins University, Baltimore, MD .............................................................................................................. 31

TOE 5:20-5:35 Generating MRI Contrasts in Rotating Frames of Rank 1≤n≤5 in the Human Brain at 4T and Mouse Brain at 7T; Timo Liimatainen1; Silvia Mangia2; Hanne Hakkarainen1; Andrew Tyan2; Djaudat Idiyatullin2; Dennis Sorce2; Michael Garwood2; Shalom Michaeli2; 1University of Eastern Finland, Kuopio, Finland; 2CMRR, University of Minnesota, Minneapolis, MN (also poster 397) .............................. 31

TOE 5:35-5:50 Early Detection of Pancreatic Cancers & Brain Tumors by Active Feedback Magnetic Resonance; Zhao Li1; Ryan Quiroz1; Raymond Ngo1; Chaohsiung Hsu2; Yu-Hao Chen2; Clifton Shen3; Mark Girgis4; Hongxiang Hui4; Vay Go5; Yung-Ya Lin1; 1Department of Chemistry & Biochemistry, UCLA, Los Angeles, CA; 2Department of Chemistry, National Taiwan Universit, Taipei, Taiwan; 3Crump Molecular Imaging Institute, UCLA, Los Angeles, CA; 4Department of Surgery, UCLA, Los Angeles, CA; 5Center for Excellence in Pancreatic Diseases, UCLA, Los Angeles, CA ........... 31

After 6:00 pm HOSPITALITY SUITES OPEN

WEDNESDAY, APRIL 18

8:30 – 10:05 am, WEDNESDAY MORNING RESOLUTION AND SENSITIVITY

Eriks Kupce, presiding Versailles Ballroom

Abstract Page WOA 8:30-8:55 Controlled Singlet to Triplet Conversion allows Para Hydrogen Induced Polarization in

Symmetric Molecules; Hans W. Spiess; María Belén Franzoni; Lisandro Buljubasich; Kerstin Muennemann; Max Planck Institute Polymers, Mainz, Germany ................................................................ 32

WOA 8:55-9:20 Ultra High-Resolution NMR in Inhomogeneous Magnetic Fields: Two-Dimensional Long-Lived Coherence Correlation Spectroscopy; Aurélien Bornet1; Srinivas Chinthalapalli2; Takuya Segawa1; Riddhiman Sarkar3; Sami Jannin1; Geoffrey Bodenhausen1; 1Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland; 2Indian Institute of Technology, New Delhi, India; 3University of Southampton, Southampton, United Kingdom ............................................................................................ 32

WOA 9:20-9:35 Hyperpolarized Singlet State NMR; Giuseppe Pileio1; Lynda J. Brown1; Michael Tayler1; Christoffer Laustsen2, 3; Richard C. D. Brown1; Jan Henrik Ardenkjaer-Larsen2, 4; Malcolm Levitt1; 1University of Southampton, Southampton, UK; 2The Technical University of Denmark, Lyngby, DK; 3Aarhus University, Aarhus, DK; 4GE Healthcare, Broendby, DK ............................................................................. 32

WOA 9:35-9:50 Fast Reconstruction of 0.8% Non-Uniformly Sampled 4D Methyl-Methyl NOESY by Iterative Soft Thresholding; Sven G. Hyberts; Alexander G. Milbradt; Gerhard Wagner; Dept. Biol. Chem. & Mol. Pharmacologie, Boston, MA (also poster 398) .................................................................................... 32

WOA 9:50-10:05 Helium-Cooling and -Spinning Dynamic Nuclear Polarization-Enhanced Solid-State NMR at 14 T and 30 K; Yoh Matsuki1; Keisuke Ueda1; Toshitaka Idehara2; Ryosuke Ikeda2; Kosuke Kosuga2; Isamu Ogawa2; Shinji Nakamura3; Mitsuru Toda3; Takahiro Anai3; Toshimichi Fujiwara1; 1Osaka Univ, Suita, Japan; 2University of Fukui, Fukui, Japan; 3JEOL RESONANCE Inc, Tokyo, Japan ........................ 32

10:15 – 10:45 am BREAK

WEDNESDAY, APRIL 18, continued

10:45 am – 12:20 pm, WEDNESDAY MORNING SMALL MOLECULES Yulan Wang, presiding

Versailles Ballroom Abstract Page WOB 10:45-11:10 FAST-NMR: Functional Annotation Using Chemical Probes; Robert Powers; University of

Nebraska-Lincoln, Lincoln, NE .................................................................................................................... 33

WOB 11:10-11:35 Fermentanomics: Using NMR Spectroscopy to Improve Cell Culture Performance.; Scott Bradley; Anli Ouyang; Jennifer Purdie; Tim Smitka; Tongtong Wang; Andreas Kaerner; Eli Lilly and Company, Indianapolis, IN .......................................................................................................................... 33

WOB 11:35-11:50 Progress in Spin-Diffusion-Guided Structure Determination of Complexes of Small Molecules and Large Targets using INPHARMA, STD, tr-NOE, Chemical Shifts and DNP; Marcel Reese1, 7; Victor Sánchez-Pedregal1; Jens Meiler2; Marcel Blommers3; Youngbok Lee6; Karel Kubicek1; Haifeng Zeng6; Melanie Wegstroth1; Donghan Lee1; Adam Mazur1; Jens Pilger1; Peter Monecke4; Stefan Bartoschek4; Alexander Schiffer4; Ulrich Wendt4; Stefan Becker1; Christian Hilty6; Teresa Carlomagno5; Christian Griesinger1; 1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Vanderbilt University, Nashville, TN; 3Novartis Institutes for BioMedical Research, Basel, Switzerland; 4Sanofi-Aventis Deutschland GmbH, Frankfurt am Main, Germany; 5EMBL Heidelberg, Heidelberg, Germany; 6Center for Biological NMR, College Station, TX; 7Massachusetts Institute of Technology, Cambridge, MA ....................................................................................................................... 33

WOB 11:50-12:05 Avoiding Strong Coupling Effects in 1JCH Measurements; Bingwu Yu; Daron Freedberg; CBER/FDA, Bethesda, MD .......................................................................................................................... 33

WOB 12:05-12:20 Chemical Shift Modulations from Fully Refocused Spin-Echo Sequences: the Selective Dynamical Recoupling Experiment; Pieter Ernst Scholtz Smith1; Guy Bensky1; Gonzalo Agustin Alvarez2; Gershon Kurizki1; Lucio Frydman1; 1Weizmann Institute of Science, Rehovot, Israel; 2Dortmund University, Dortmund, Germany ................................................................................................ 33

10:45 am – 12:20 pm, WEDNESDAY MORNING EXOTICA

Dieter Suter, presiding Trianon Ballroom

Abstract Page WOC 10:45-11:10 Optically Re-Writable Patterns of Nuclear Magnetization in Gallium Arsenide; Jeffrey Reimer;

UC Berkeley, Berkeley, CA ......................................................................................................................... 34

WOC 11:10-11:35 Earth's Field MRI in the Freshman Physics Lab: Hardware, Software and Strategy; Carl A. Michal; University of British Columbia, Vancouver, Canada ........................................................................ 34

WOC 11:35-11:50 SUCCESS: Suppression of Undesired Chemicals using Contrast-Enhancing Singlet States; Stephen Devience1; Ronald Walsworth2, 3; Matthew Rosen4, 5; 1Harvard University Department of Chemistry and Che, Cambridge, MA; 2Harvard-Smithsonian Center for Astrophysics, Cambridge, MA; 3Harvard University Department of Physics, Cambridge, MA; 4Harvard Medical School, Boston, MA; 5Martinos Center for Biomedical Imaging, Boston, MA (also poster 399) .................................................... 34

WOC 11:50-12:05 Comprehensive Multiphase NMR Spectroscopy: A Powerful Approach for Natural Samples; Andre J Simpson1; Denis Courtier-Murias1; Ronald Soong1; Hussain Masoom1; Adolfo Botana1; James Longstaffe 1; Hashim Farooq1; Myrna J Simpson1; Werner E. Maas2; Michael Fey2; Brian Andrew2; Jochem Struppe2; Howard Hutchins2; Sridevi Krishnamurthy2; Rajeev Kumar3; Martine Monette3; Henry J. Stronks3; Alan Hume3; 1University of Toronto, Scarborough, ON; 2Bruker Biospin, Billerica, MA; 3Bruker BioSpin Canada, Milton, ON ..................................................................................... 34

WOC 12:05-12:20 Solid State NMR at Cryogenic Temperature; Maria Concistre1; Ole G. Johannessen1; Salvatore Mamone1; Riddhiman Sarkar1; Elisa Carignani2; Mark Denning1; Yasujiro Murata3; Judy Y. Chen4; Nicholas J. Turro4; Marina Carravetta1; Philip T. Williamson1; Marco Geppi2; Maithan K. Al-Mosawi1; Carlo Beduz1; Yifeng Yang1; Malcolm Levitt1; 1University of Southampton, Southampton, United Kingdom; 2University of Pisa, Pisa, IT; 3Kyoto University, Kyoto, JP; 4Columbia University, New York ...... 34

WEDNESDAY, APRIL 18, continued



Authors of odd numbered spaces (001, 003, etc) present. Posters 001 - 306, Atrium. Posters 307 - 412, Chopin Ballroom

4:00 – 5:50 pm, WEDNESDAY AFTERNOON MOTION AND DYNAMICS J. Patrick Loria, presiding

Versailles Ballroom Abstract Page WOD 4:00-4:25 RNA-based Regulation Elements Studies by NMR Spectroscopy; Harald Schwalbe1; Jorg

Rinnenthal1; Hannah Steinert1; Dominik Wagner1; Anke Reining1; Boris Furtig1; Janina Buck1; Anna Wacker1; Senada Nozinovic1; Thorsten Marquardsen2; 1Univ of Frankfurt, Frankfurt, Germany; 2Bruker Biospin, Rheinstetten, Germany ..................................................................................................... 35

WOD 4:25-4:50 Ligand-Mediated Conformational Dynamics in the Catalytic Function of the Alpha Subunit of Tryptophan Synthase; David Boehr; Jennifer Axe; Penn State, University Park, PA ................................ 35

WOD 4:50-5:05 High-Pressure NMR Reveals that the Native State of Proteins Contains the "Dry" Molten Globule; Yinan Fu1; Vignesh Kasinath1; Veronica Moorman1; Nathaniel Nucci1; Vincent Hilser2; Joshua Wand1; 1Univ of Pennsylvania, Philadelphia, PA; 2Johns Hopkins University, Baltimaore, MD (also poster 400) ......................................................................................................................................... 35

WOD 5:05-5:20 Motion of Disordered Protein Studied by PREs, 15N Relaxation, and MD Simulations: How Fast is Segmental Diffusion in Denatured Ubiquitin?; Yi Xue; Nikolai R. Skrynnikov; Purdue University, West Lafayette, IN ....................................................................................................................................... 35

WOD 5:20-5:35 Excited States of the HIV Dimerization Initiation Site RNA revealed by NMR; Katja Petzold; Hashim Al-Hashimi; University of Michigan, Dept. Biophysics, Ann Arbor, MI ............................................ 35

WOD 5:35-5:50 Electrostatic Interactions and Description of the Encounter Complex in Binding of Proline Rich Motifs to a SH3 Domain; Erick Alejandro Meneses Ramirez; Anthony Mittermaier; McGill University, Department of Chemistry, Montreal, Canada ............................................................................ 35

4:00 – 5:50 pm, WEDNESDAY AFTERNOON MRI/MRS

Daniel Vigneron, presiding Trianon Ballroom

Abstract Page WOE 4:00-4:25 MR Metabolic Imaging of Cancer; Sarah Nelson, UCSF, San Francisco, CA WOE 4:25-4:50 Revisiting Decades-Old Spin Physics to Improve Modern Magnetic Resonance Imaging;

Warren S. Warren; Duke University, Durham, NC ....................................................................................... 36

WOE 4:50-5:05 2D Ultrafast J-resolved MRS Sequence with 3D Localization: an in vitro Validation on a 7T Imaging System; Serge Akoka1; Tangui Roussel2; Patrick Giraudeau1; Hélène Ratiney2; Sophie Cavassila2; 1CEISAM, UMR 6230, CNRS/Université de Nantes, Nantes, France; 2CREATIS, UMR 5220, Universite de Lyon, Lyon, France (also poster 401) .......................................................................... 36

WOE 5:05-5:20 Mapping the Phase Diagram for Anomalous Diffusion in the Rat Brain at 17.6 T; Carson Ingo; University of Illinois at Chicago, Chicago, IL ................................................................................................ 36

WOE 5:20-5:35 Measuring the Permeability and Stability of Microcapsules with Dynamic NMR Microimaging; Stefan Henning1; Daniel Edelhoff1; Benedikt Ernst1; Sabine Leick2; Heinz Rehage2; Dieter Suter1; 1Exp. Physics III, TU Dortmund, Dortmund, Germany; 2Phys. Chemistry II, TU Dortmund, Dortmund, Germany ...................................................................................................................................................... 36

WOE 5:35-5:50 Ovarian Cancer Detection Using Hyperpolarized 13C-Pyruvate with MR Imaging and Spectroscopy; Mehrdad Pourfathi1; Stephen J. Kadlecek1; Harrila Profka1; Hoora Shaghaghi1; Moses Darpolor1; Kiarash Emami1; Nicholas N. Kuzma1; Jan H. Ardenkjær-Larsen2; Rahim R. Rizi1; Janet A. Sawicki3; 1University of Pennsylvania, Philadelphia, PA; 2GE Healthcare, Brøndby, Denmark; 3Lankenau Institute for Medical Research, Wynnewood, PA ...................................................... 36

After 6:00 pm, HOSPITALITY SUITES OPEN

THURSDAY, APRIL 19

8:30 – 10:05 am, THURSDAY MORNING EXOTICA MRI

Joseph Helpern, presiding Versailles Ballroom

Abstract Page ThOA 8:30-8:55 Balanced SSFP as a Marker of Magnetic Susceptibility in the Brain; Karla Miller; FMRIB Centre,

Oxford , United Kingdom ............................................................................................................................. 37

ThOA 8:55-9:20 Nanoscale Spin Imaging; Jorg Wrachtrup; Universitat Stuttgart, Stuttgart, Germany .............................. 37

ThOA 9:20-9:35 Combining Double Quantum Filtering and Magnetization Transfer with UTE to Obtain Images Based on Macromolecular Characteristics; Uzi Eliav1; Michal Komlosh2; Peter J. Basser2; Gil Navon1; 1Tel Aviv University, Tel Aviv, Israel; 2National Institutes of Health, Bethesda, MD ....................... 37

ThOA 9:35-9:50 In-situ 7Li MRI of Li-ion Batteries; S. Chandrashekar1; Nicole Trease2; Hee-Jung Chang2; Alexej Jerschow1; Clare P. Grey3; 1new york university, New York, NY; 2stony brook university, stony brook, NY; 3University of Cambridge, Cambridge, United Kingdom (also poster 402) ........................................... 37

ThOA 9:50-10:05 Long Lived Coherent Response Signal: New Echoes and Bone Signals; Boyang Zhang1; Jae-Seung Lee1; Anatoly Khitrin2; Alexej Jerschow1; 1New York University, New York, NY; 2Kent State University, Kent, OH .................................................................................................................................... 37

10:15 – 10:45 am BREAK

THURSDAY, APRIL 19, continued

10:45 am – 12:20 pm, THURSDAY MORNING SCREENING

Istvan Pelczer, presiding Versailles Ballroom

Abstract Page ThOB 10:45-11:10 Screening Stress-induced Systems Metabolic Responses using NMR; Huiru Tang; Yulan Wang;

Wuhan Institute of Physics and Mathematics, Wuhan, China ..................................................................... 38

ThOB 11:10-11:35 New insights into Food Quality Control by NMR Based Screening; Manfred Spraul; Hartmut Schaefer; Birk Schuetz; Fang Fang; Eberhard Humpfer; Bruker BioSpin, Rheinstetten, Germany ............. 38

ThOB 11:35-11:50 Automating the Processing and Analysis of High Throughput Ligand-Protein Binding Spectra within the MestReNova System; Chen Peng1; Manuel Perez1; Juan Carlos Cobas1; Xiaolu Zhang2; Jasna Fejzo2; Jaison Jacob2; Andreas Lingel3; 1Mestrelab Research, Santiago de Compostela, Spain; 2Novartis Institutes for BioMedical Research, Inc., Cambridge, MA; 3Novartis Institutes for Biomedical Research, Emeryville, CA (also poster 403) ................................................................................................ 38

ThOB 11:50-12:05 Metabolomics of Intact Tissues: Discrimination Between Different Regions of Osteolytic Lesions in Multiple Myeloma Patient using 1H HRMAS NMR spectra; Silvia Mari1, 4; Francesca Fontana1; Jose Garcia Manteiga1; Edoardo Gaude1; Simone Cenci1; Enrico Caneva2; Giovanna Musco1; Stanislav Sykora3; Juan Carlos Cobas Gomez5; 1S. Raffaele Scientific Institute, Milan, IT; 2Università degli Studi di Milano, Milan, IT; 3Extra Byte, Castano Primo, IT; 4R4R, Rodano, IT; 5Mestrelab Research, Santiago de Compostela, ES (also poster 404) ....................................................... 38

ThOB 12:05-12:20 Boosting Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States; Nicola Salvi; Aurélien Bornet; Roberto Buratto; Geoffrey Bodenhausen; Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland (also poster 405) ................................................................................... 38

10:45 am – 12:20 pm, THURSDAY MORNING

SOLIDS II Marc Baldus, presiding

Trianon Ballroom Abstract Page ThOC 10:45-11:10 Conformational Exchange Processes in Membrane Proteins and Enzymes by Solid State NMR;

Ann Mcdermott; Manasi Bhate; Benjamin J Wylie; Columbia University, New York, NY ............................. 39

ThOC 11:10-11:35 Amyloid Fibril Structures: Methods and Results; Wei Qiang; Junxia Lu; Kan-Nian Hu; Wai-Ming Yau; Alexey Potapov; Kent Thurber; Robert Tycko; National Institutes of Health, Bethesda, MD ............... 39

ThOC 11:35-11:50 Solid-State NMR of Viral Particles; Emeline Barbet-Massin1; Michele Felletti1; Stefan Jehle1; Anne Lesage1; Arne Linden2; Sascha Lange2; Trent Franks2; Umit Akbey2; Hartmut Oschkinat2; Kaspars Tars3; Guillaume Communie4; Robert Schneider4; Malene R. Jensen4; Martin Blackledge4; Lyndon Emsley1; Guido Pintacuda1; 1CRMN / ENS Lyon, Villeurbanne, France; 2FMP Berlin, Berlin, Germany; 3Biomedical Research and Study Center, Riga, Latvia; 4IBS, Grenoble, France ......................................... 39

ThOC 11:50-12:05 Supramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and Molecular Dynamics Simulations; Markus Weingarth1; Christian Ader1; Adrien Melquiond1; Deepak Nand1; Olaf Pongs2; Stefan Becker3; Alexandre M. J. J. Bonvin1; Marc Baldus1; 1Utrecht University, Bijvoet Center, Utrecht, Netherlands; 2Instut fur Neurale Singnalverabeitung,Univ Hamburg, Hamburg, Germany; 3Max Planck Insitute for Biophysical Chemistry, Gottingen, Germany (also poster 406) ......................................................................................................................................... 39

ThOC 12:05-12:20 Dual Acquisition Magic Angle Spinning (DUMAS) Solid-State NMR: A New Approach to Simultaneous Acquisition of Multi Dimensional Spectra of Biomacromolecules; Gopinath Tata1,

2; Gianluigi Veglia1, 2; 1University of Minnesota, Minneapolis, MN; 2University of Minnesota, Minneapolis, MN (also poster 407) .............................................................................................................. 39


2:00 – 3:45 pm

POSTER SESSION Abstracts begin on page 44. Authors of even numbered spaces (002, 004, etc) present.

Posters 001 - 306, Atrium. Posters 307 - 412, Chopin Ballroom Remove posters at 3:45 pm

THURSDAY, APRIL 19, CONTINUED

4:00 – 5:50 pm, THURSDAY AFTERNOON SOFTWARE AND HARDWARE

Frank Engelke, presiding Versailles Ballroom

Abstract Page ThOD 4:00-4:25 Characterization of Free Energy Landscapes of Proteins using NMR Spectroscopy; Michele

Vendruscolo, University of Cambridge, Cambridge, United Kingdom .......................................................... 40

ThOD 4:25-4:50 Probing Mysteries of NMR Stark Spectroscopy with new Hardware & old Software; Jim Kempf; Matthew Tarasek; David Goldfarb; Rensselaer Polytechnic Inst., Troy, NY ............................................... 40

ThOD 4:50-5:05 High Spin-Lock (> 4 kHz) for R1rho using a Cryogenically Cooled Probe.; David Ban1; Alvar Gossert2; Helena Kovacs3; Karin Giller1; Stefan Becker1; Christian Griesinger1; Donghan Lee1; 1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Novartis Institutes of BioMedical Research, Basel, Switzerland; 3Bruker BioSpin AG, Fällanden, Switzerland (also poster 408) .................. 40

ThOD 5:05-5:20 Determination of a High-Resolution Model of the Type-III Secretion System Needle Using Solid-State NMR Data and Rosetta Modeling.; Nikolaos Sgourakis5; Antoine Loquet1, 2, 3; Adam Lange4; David Baker5; 1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 3Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 4Max Planck Institute, Goettingen, Germany; 5University of Washington, Seattle, WA ............................................................................................................................. 40

ThOD 5:20-5:35 Improved Knowledge-Based Torsion-Angle Potentials Yield Higher-Quality NMR Structures of Proteins; Guillermo A. Bermejo; G. Marius Clore; Charles D. Schwieters; National Institutes of Health, Bethesda, MD (also poster 409)...................................................................................................... 40

ThOD 5:35-5:50 High Pressure MAS NMR; Flaviu Turcu; David Hoyt; Jesse Sears; Kevin Rosso; John Loring; Jian Zhi Hu; Pacific Northwest National Laboratory, Richland, WA .................................................................... 40

4:00 – 5:50 pm, THURSDAY AFTERNOON

ENC FOCUS: NMR IN LATIN AND SOUTH AMERICA A. J. Shaka, presiding

Trianaon Ballroom Abstract Page ThOE 4:00-4:25 Dynamically Induced Decoherence Observed through a Loschmidt Echo in NMR; Patricia

Rebeca Levstein1, 2; Claudia Marina Sánchez1; Ana Karina Chattah1, 2; Rodolfo Hector Acosta1, 2; Horacio Miguel Pastawski1, 2; 1FAMAF, Universidad Nacional de Córdoba, Córdoba, Argentina; 2IFEG-CONICET, Córdoba, Argentina ........................................................................................................ 41

ThOE 4:25-4:50 Multi-quantum Echoes in GdAl2 Zero-field NMR; Joao Teles; Jose R. Tozoni; Rodrigo Oliveira-Silva; Ruben Auccaise; Christian Rivera-Ascona; Edson L. G. Vidoto; Tito J. Bonagamba; IFSC - USP, Sao Carlos, Brazil .............................................................................................................................. 41

ThOE 4:50-5:05 How to Measure the Performance of Automated Structure Verification Systems using Negative Control Structures; Gonzalo Hernández; Vis Magnetica, Montevideo, Uruguay (also poster 410) ........... 41

ThOE 5:05-5:20 Synthesis and Characterization of 6-bromo-4-(4-chloro-phenyl)-8-methoxy-quinoline by NMR Spectroscopy and X-Ray Diffraction; Ligia Llovera; USB, Caracas, Venezuela .................................... 41

ThOE 5:20-5:35 Role of Excited States Characterized by NMR in the Catalytic Cycle of Yeast Thioredoxin 1-Thermodynamic Characterization of Water Permeation; Luciana Elena Machado; Federal University of Rio de Janeiro, Rio De Janeiro, Brazil .................................................................................... 41

ThOE 5:35-5:50 Analysis of the Folding Functions and a Dynamic Approach to the Problem of Optimizing Spectral Widths in 2D NMR Experiments; José Félix Gómez-Reyes; Armando Ariza-Castolo; CINVESTAV, México D.F., México .............................................................................................................. 41

6:30 – 8:00 pm, BANQUET, Chopin Ballroom (ticket required)

8:00 – 9:00 pm, After Dinner Program, A.J. Shaka, presiding, Versailles Ballroom Richard R. Ernst ENC: A Major Stimulator in My Scientific Life Open to all conferees. Vendor Raffle – must be present to win.

FRIDAY, APRIL 20

8:30 – 10:10 am, FRIDAY MORNING FRONTIERS

Tatyana Polenova, presiding Versailles Ballroom

Abstract Page FOA 8:30-8:55 NMR with a Single Proton; Stefan Ulmer; Holger Kracke; RIKEN Advanced Science Institute,

Saitama , Japan ........................................................................................................................................... 42

FOA 8:55-9:20 Cellular Solid-State NMR Spectroscopy; Marie Renault; Martine Bos; Eline Koers; Ria Tommassen-van Boxtel; Mohammed Kaplan; Jan Tommassen; Marc Baldus; Utrecht University, Utrecht, Netherlands ................................................................................................................................... 42

FOA 9:20-9:35 Molecular Spins: a New Frontier of Chemical Physics and Magnetic Resonance?; Stanislav Sykora; Extra Byte, Castano Primo, Italy..................................................................................................... 42

FOA 9:35-9:50 Optically Detected NMR Relaxometry in Low Magnetic Field; Paul Ganssle1, 2; Hyun Doug Shin1,

2; Scott Seltzer1, 2; Vikram S. Bajaj1, 2; Dmitry Budker2, 3; Svenja Knappe4; John Kitching4; Alex Pines1,

2; 1UC Berkeley, Dept. of Chemistry, Berkeley, CA; 2Lawrence Berkeley National Labs, Berkeley, CA; 3UC Berkeley, Dept. of Physics, Berkeley, CA; 4Time and Frequency Division, NIST, Boulder, CO ........... 42

FOA 09:50-10:05 A Spinning Permanent Magnet for Magic Angle Field Turning; Cedric Hugon2; Dimitrios Sakellariou1; 1CEA Saclay, Gif-Sur-Yvette, France; 2École Normale Supérieure, 24 rue Lohmond, Paris, France ............................................................................................................................................... 42

10:15 – 10:45 am BREAK

10:45 am – 12:20 pm, FRIDAY MORNING LARGE SYSTEMS

Chad Rienstra, presiding Versailles Ballroom

Abstract Page FOB 10:45-11:10 Solution NMR Studies of Membrane Transporters; James Chou; Harvard Medical School, Boston,

MA ............................................................................................................................................................... 43

FOB 11:10-11:35 Parameterization of Solvent-Protein Interaction and Its Use on NMR Protein Structure Determination; Yu Wang1; Charles D. Schwieters2; Nico Tjandra1; 1NHLBI, National Institutes of Health, Bethesda, MD; 2CIT, National Institutes of Health, Bethesda, MD .................................................. 43

FOB 11:35-11:50 Experiments Optimized for Rotationally Aligned Solid-State NMR of Membrane Proteins in Proteoliposomes; Bibhuti Das; Stanley J. Opella; University of California, San Diego, La Jolla, CA ........ 43

FOB 11:50-12:05 Magic Angle Spinning Dynamic Nuclear Polarization NMR at 700 MHz/460 GHz; Vladimir K. Michaelis1; Eugenio Daviso1, 2; Evgeny Markhasin1; Alexander B. Barnes1; Emilio A. Nanni1; Sudheer K. Jawla1; Ajay Thakkar1; Ronald DeRocher1; Judith Herzfeld2; Richard J. Temkin1; Robert G. Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA; 2Brandeis University, Waltham, MA (also poster 411) .................................................................................................................................................. 43

FOB 12:05-12:20 Paramagnetic mapping of the 116 kDa Ca2+ATPase/phospholamban membrane protein complex in lipid bilayers by solid state NMR spectroscopy; Martin Gustavsson1; Raffaello Verardi1; Nathaniel J Traaseth2; Gianluigi Veglia1; 1University of Minnesota, Minneapolis, MN; 2New York University, New York, NY (also poster 412) ........................................................................................ 43

Adjourn

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10:45 am – 12:20 pm, MONDAY MORNING BIOMOLECULES STRUCTURE AND FUNCTION

A. J. Shaka, presiding Versailles

MOB 10:45-11:10 Proteins in Flagrante

Dorothee Kern; Brandeis University, Boston, MA Understanding biological function, such as the fascinating rate acceleration of enzymes, or the sophisticated action of membrane transporters, has been a long-standing challenge. Despite remarkable information generated using chemical tools in the last 100 years, complemented more recently with structural and computational approaches, we cannot yet identify with a complete energy inventory how ANY enzyme works. The secret of enzymes lies in their ability to partition energetic contributions among many atoms in a well-coordinated style. To unravel these secrets, proteins in action are spied on at atomic resolution to provide a comprehensive description of enzyme catalysis in the form of an energy landscape.

MOB 11:10-11:35

The Dynamic Structure of a Viral Fusion Domain and its Interaction with Lipids from RDCs and Size-Dispersed

Relaxation Justin Lorieau; John Louis; Ad Bax; NIH, Bethesda, MD

Biological membranes present a highly fluid environment and integration of proteins into them is itself highly dynamic: proteins diffuse laterally within the plane of the membrane, and rotationally about the bilayer normal. For the influenza hemagglutinin fusion domain, which plays a key role in fusing the endosomal and viral membranes, 15N NMR relaxation for different size mixed lipid particles reveals large-amplitude, rigid-body nanosecond motions relative to the lipid bilayer. NMR data reveal that the remarkably tight hairpin structure of the fusion domain, stabilized by aliphatic H-bonds, can transiently open at low pH where membrane fusion takes place. A dynamic equilibrium between at least three structures is required to fit the NMR data.

MOB 11:35-11:50

Atomic Resolution Dynamics on the Surface of Amyloid Beta Protofibrils Probed by Dark state Exchange

Saturation Transfer (DEST) Spectroscopy Nicolas Fawzi1; Jinfa Ying1; Rodolfo Guirlando1; Dennis Torchia2; Marius Clore1; 1NIDDK, NIH, Bethesda, MD;

2NIDCR, NIH, Bethesda, MD Exchange dynamics between molecules free in solution and bound to the surface of large supramolecular structures are important in many phenomena in biology and materials science. We describe a novel and generally applicable solution NMR technique, known as Dark-state Exchange Saturation Transfer (DEST), to probe such exchange phenomena with atomic resolution. This is illustrated by the exchange reaction between amyloid beta monomers and polydisperse, NMR invisible ('dark') protofibrils. The 15N-DEST experiment imprints with single residue resolution dynamic information on the protofibril-bound species in the form of 15N transverse relaxation rates (15N-R2) and exchange kinetics between monomers and protofibrils onto the easily observed two-dimensional 1H-15N correlation spectrum of the monomer.

MOB 11:50-12:05 Structure and Dynamics of a Microcrystalline

Metalloprotein by Solid-state NMR : Proton-detection, Ultra-fast MAS and Paramagnetic Restraints

Michael J. Knight1; Andrew Pell1; Ivano Bertini2; Isabella C. Felli2; Leonardo Gonnelli2; Roberta Pierattelli2; Torsten

Herrmann1; Lyndon Emsley1; Guido Pintacuda1; 1ENS-Lyon, Villeurbanne, France; 2CERM - University of Florence,

Florence, Italy We show how proton-detected methods, facilitated by ultra-fast MAS at 60 kHz, high magnetic fields and perdeuteration allow the rapid and accurate site-specific measurements of nuclear relaxation rates in a 150-residue microcrystalline metalloprotein by solid-state NMR, and show how such data can be applied to both the structure determination and characterization of backbone dynamics. The particular protein we study contains a Cu ion and a Zn ion. By taking site-specific measurements of the 15N and 13C R1 in both the Cu(I) (diamagnetic) and Cu(II) (paramagnetic) states, we obtain paramagnetic relaxation enhancements (PREs) and apply these, together with 1H-1H distance restraints, to structure calculation. The PREs reduce the structure RMSD by 50%.

MOB 12:05-12:20

Characterizing the Role of VDAC1's N-Terminus in Channel Gating with Magic Angle Spinning NMR

Matthew T. Eddy1; Oscar Hermida2; Lindsay Clark1; Loren Andreas1; Yongchao Su1; Patrick van der Wel1; Gerhard

Wagner3; Tatiana Rostovtseva2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA;

2National Institutes of Health, Bethesda, MD; 3Harvard Medical School, Boston, MA

VDAC1 is a 32 kDa integral membrane protein that controls transport of metabolites across the outer mitochondrial membrane. The mechanism of VDAC1’s characteristic ability to switch or “gate” between “open” and “closed” states remains unsolved on a structural level. In particular, the N-terminus has been proposed to be critical for gating yet structural evidence for this role is lacking. Here we report direct distance measurements between the N-terminus and other regions of the protein using Proton Assisted Recoupling in uniformly and selectively labeled VDAC1 reconstituted in lipid bilayers. We also present correlation experiments that characterize the role of the N-terminus in channel gating by probing possible conformational changes induced by pH dependence, temperature dependence, lipid phase dependence, and posttranslational modifications.

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4:00 – 5:50 pm, MONDAY AFTERNOON SOLIDS I

Philip Grandinetti, presiding Versailles

MOD 4:00-4:25 NMR Crystallography in the Enzyme Active Site of

Tryptophan Synthase Leonard J Mueller; University of California, Riverside, CA

Chemical level details such as protonation and hybridization state are critical for understanding enzyme mechanism and function. Here we make use of solid-state NMR in combination with X-ray crystallography and computational chemistry to determine chemically-rich crystal structures and probe dynamics of several intermediates in the multistep catalytic cycle of tryptophan synthase. Various models of charge and protonation state for the substrate and nearby catalytic residues can be distinguished by their calculated effect on the chemical shifts, measured at specifically 13C- and 15N-labeled positions on the substrate. For the indoline quinonoid intermediate, our results suggest the importance of an equilibrium between tautomeric forms of the substrate, with the protonation state of the major isomer directing the next catalytic step.

MOD 4:25-4:50

SSNMR Investigations of Proton Conduction and Membrane Curvature Generation by an Ion Channel

Mei Hong; Iowa State, Ames, IA MAS NMR is used elucidate the ion conduction kinetics and membrane interaction of the influenza M2 proton channel. 15N NMR lineshapes indicate proton exchange of the crucial histidine residue. The exchange-induced 15N T2 was analyzed by a new T2 theory for anisotropic solids under 1H decoupling and MAS, yielding the rate of proton exchange. Acid dissociation constants of the histidine tetrad were measured to give relative single-channel conductivities of the different protonation states. An amphipathic helix of M2 was found to cause high-curvature membrane domains. M2 localization in the membrane was determined from indirectly detected 1H T2 relaxation times and by 2D 1H-31P correlation experiments. The peptide partitions into the high-curvature domain, which perturbs drug binding to the transmembrane pore.

MOD 4:50-5:05

MAS NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A

Loren Andreas1; Matthew T. Eddy1; James Chou2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge,

MA; 2Harvard Medical School, Boston, MA The helical M2 tetramer has been the subject of intense scrutiny as a model proton selective channel and potential drug target. Existing aminoadamantyl inhibitors bind to the protein, but are ineffective against the widespread S31N mutant. We have assigned spectra of the drug-resistant S31N mutant of M218-60 using 3D 15N-13C-13C ZF-TEDOR-RFDR spectra. Assignments reveal two sets of resonances, indicating that the tetramer assembles as a dimer of dimers, similar to the wild type channel. The two sets of chemical shifts reveal a difference in the TALOS+ predicted torsion angles for the resistance residue N31. In contrast to wild type M218-60, shift changes are minimal with addition of inhibitor, providing a negative control for functional relevance of shift changes in WT.

MOD 5:05-5:20 S-RESPDOR for Inter-Nuclear Distance Measurement

between Spin-1/2 and Quadrupolar Nuclei Jean Paul Amoureux; Xingyu LU; Olivier Lafon; Frederique

Pourpoint; Lille university, Villeneuve D'ascq, France S-RESPDOR uses a symmetry-based recoupling sequence on the observed spin-1/2 channel, and a single saturation pulse on the quadrupolar channel. This non-dipolar-truncated method, which presents the advantage of one single general analytical formula for all spin values, displays high robustness to: (1) homo-nuclear dipolar interactions, (2) rf-field inhomogeneity, (3) shielding, and (4) relative orientations of various microscopic interactions. The method is not rf-demanding, even in case of strong CQ and fast spinning speeds. S-RESPDOR has been demonstrated with several pairs of nuclei: 31P-51V, 13C-14N, 13C-27Al and 13C-67Zn, as well as 13C-17O with natural 13C abundance and 30% 17O enrichment. In all cases, the distances determined with S-RESPDOR were in perfect agreement with those obtained from XRD.

MOD 5:20-5:35

Protein Fold Determined by Paramagnetic Magic-Angle Spinning Solid-State NMR Spectroscopy

Ishita Sengupta; Graduate Student, Columbus, OH We present the determination of the backbone fold for a model 56-residue protein, GB1, by solid-state NMR using ~230 longitudinal 15N paramagnetic relaxation enhancement restraints measured for a set of six GB1 mutants modified with cysteine-EDTA-Cu+2 tags.

MOD 5:35-5:50

Developing a Fully Broadband Cross-Polarization Experiment using Adiabatic Pulses: Theory and Experiment for the BRAIN-CP Pulse Sequence

Robert W. Schurko1; Kristopher J. Harris1; Bryan E.G. Lucier1; Adonis Lupulescu2; Lucio Frydman2; 1University of Windsor,

Windsor, Canada; 2Weizmann Institute, Rehovot, Israel In recent years, a significant amount of research has gone into improving cross polarization (CP) experiments for standard nuclides (13C, 15N, 29Si, 31P, etc.). However, the challenge of improving the limited excitation bandwidth of conventional CP for use in acquiring broad powder patterns created by the large, anisotropic interactions has so far remained unaddressed. We introduce the BRoadband Adiabatic INversion Cross Polarization, BRAIN-CP, pulse sequence and demonstrate that it yields an approximately five- to ten-fold increase in the excitation bandwidth over conventional CP. Experiments using 1H nuclei to polarize 119Sn, 199Hg, 207Pb, or 195Pt nuclei with excitation bandwidths greater than 0.5 MHz will be presented.

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4:00 – 5:50 pm, MONDAY AFTERNOON DETECTION

James Prestegard, presiding Trianon

MOE 4:00-4:25 Detection of Spin Polarization in Semiconductors with

Optical-Pumping Dustin Wheeler1; Erika Sesti1; Wieland Worthoff2; Christopher

Stanton3; Sophia E. Hayes1; 1Washington University, Saint Louis, MO; 2TU Dortmund, Dortmund, Germany; 3University of

Florida, Gainesville, FL Optically-pumped NMR (OPNMR) and optically-detected NMR (ODNMR) both utilize optical-pumping of conduction electrons in semiconductors to generate unique signals. In OPNMR, we use radio-frequency detection of nuclear spins as reporters of the electron spin polarization. In complementary measurements, ODNMR in semiconductors uses magnetic resonance in conjunctions with polarized photoluminescence from recombination of conduction electrons with holes in the valence band. We will discuss results from these measurements in AlGaAs/GaAs multiple quantum well samples.

MOE 4:25-4:50

Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy

Anne Lesage; University of Lyon, High Field NMR Center, Villeurbanne, France

NMR spectroscopy is the method of choice for characterizing surfaces whenever possible, but the detection limit of NMR is far too low to allow many modern materials to be examined. Because it provides dramatic sensitivity enhancement, solid-state DNP NMR is currently emerging as a powerful tool to study samples previously inaccessible to NMR. We have recently shown how DNP could be used to selectively enhance the NMR signals from surfaces (DNP SENS). This approach provides remarkable signal enhancements (up to a factor 100 for 13C or 29Si) making complete characterization of surface species possible. The latest developments in this field will be presented, including the introduction of new polarizing agents and the first applications of DNP SENS to catalytic systems.

MOE 4:50-5:05

Near-Field Microprobes : NMR and MRI Applications El Mohamed Halidi1; Eric NATIVEL2; Laurent Mahieu-

Willame3; Paul C. Stein4; Nadia Bertin5; Rémy Schimpf6; Michel Zanca1; Christophe Goze-Bac1; 1NanoNMRI UM2-

CNRS L2C UMR5221, Montpellier, France; 2UM2-CNRS IES UMR5214, Montpellier, France; 3CNRS CREATIS UMR5220,

Lyon, France; 4FKF-SDU, Campusvej, Odense, Denmark; 5PHS INRA, Avignon, France; 6RS2D, Bischwiller, France

The principle of NMR is based on the detection of the magnetization originating from the spin of atomic nuclei. The spin is polarized by a static magnetic field and excited by radiofrequency pulses (wavelength about one meter), that tilt the axis of the magnetization. When the magnetization returns to equilibrium, with a classical receiving antenna, we detect the electromagnetic field. This contribution, we propose the use of a micrometer-sized probe positioned in the vicinity of the object of interest, at a distance shorter than the wavelength of the radiated NMR signal. Our microprobe presents innovative characteristics: a capacitive coupling (electric field component) and reduced dimensions for an

accurate positioning, which ensure the detection of NMR signal from the sample.

MOE 5:05-5:20

Design Considerations for High-Temperature-Superconducting NMR Probes

Vijaykumar Ramaswamy1; Jerris Hooker2; Richard Withers3; Robert Nast3; William Brey2; Arthur Edison1, 2; 1University of Florida, Gainesville, FL; 2National High Magnetic Field Lab, Tallahassee, FL; 3Agilent Technologies, Santa Clara, CA

NMR is inherently a low-sensitivity technique because of the low equilibrium polarization. A very cost- effective means of increasing the sensitivity of NMR is to design highly sensitive RF probes. The overall goal of the current project is to develop high-temperature-superconducting NMR probes with extremely high mass sensitivities for both the 13C and 1H channels. In this work, we describe a method to characterize candidate coil designs using electromagnetic simulation to predict their Signal to Noise ratio and level of salt tolerance. We also describe the effect of changes in the coil orientation and symmetry on the E-field. The optimal coil configuration for maximum sensitivity is dependent on the shape and size of the sample.

MOE 5:20-5:35 PHIP Monitoring of Conformational Changes and

Stereoselective Reactions Xiang Xu1; Boyang Zhang1; Joel A Tang1, 2; Francesca Gruppi1; James Canary1; Alexej Jerschow1; 1New York

University, New York, NY; 2NHMFL FSU, Tallahassee, FL The highly cluttered and low signal-to-noise ratio spectra commonly associated with NMR spectroscopy of macromolecules makes it difficult to examine biological and chemical properties of the biomolecule. Here we demonstrate the hyperpolarization of thiostrepton and its derivatives, through a hydrogenation reaction using para-hydrogen. In addition to signal enhancements by isolating specific sites with hyperpolarization spin labels using Only Para-hydrogen Spectroscopy, a conformational change during hydrogenation reaction is observed. When using enantiomeric specific catalysts; the differences in chemical shift and peak intensity also indicate the asymmetric catalysis of the macromolecules. These results demonstrate the utility of PHIP for investigating conformational changes and stereoselective hydrogenation reactions.

MOE 5:35-5:50

First Microfabricated Inserts for Magic Angle Coil Spinning (MACS) NMR Spectroscopy

Vlad Badilita; University of Freiburg, Freiburg Im Breisgau, Germany

We report a single-chip probe for “magic angle coil spinning”-MACS magnetic resonance spectroscopy (NMR). The probe consists in a wirebonded microcoil integrated with an on-chip interdigitated capacitor. The LC-circuit consisting in the capacitor and microcoil is resonant at 700MHz enabling both wireless inductive coupling of the NMR signal and spinning for high resolution NMR. We demonstrate stable spinning up to 10 kHz of the probe containing 330nl adamantane sample. The probe successfully withstands the large centrifugal forces as well as the eddy current heating. We prove increased spectral resolution 1.5 ppm at 5 kHz rotation speed to 0.9 ppm at 10 kHz rotation speed.

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8:30 – 10:05 am, TUESDAY MORNING BIOMOLECULAR NMR

Teresa Carlomagno, presiding Versailles

TOA 8:30-8:55 NMR Detection of Structures in the HIV-1 5′-Leader RNA: Insights into the Mechanism of HIV-1 Genome Packaging

Xiao Heng; UMBC, Baltimore, MD Genome RNA dimerization and packaging of HIV-1 are mediated by interactions between the nucleocapsid (NC) domains of the viral Gag polyproteins and RNA elements within the highly conserved 5′-leader of the genome. We developed a nuclear magnetic resonance (NMR) approach that enabled direct detection of structural elements within the intact leader (712-nucleotide dimer, 230kD) that are critical for genome packaging. Our results support a packaging mechanism in which translation, dimerization, NC binding, and packaging are regulated by a common RNA structural switch.

TOA 8:55-9:20

Function of the Shwachman-Bodian-Diamond Syndrome Protein in Ribosome Assembly

Christine Hilcenko; MRC, Cambridge, United Kingdom The Shwachman-Bodian-Diamond syndrome (SBDS) protein cooperates with the GTPase elongation factor-like 1 (EFL1) to catalyze release of eukaryotic initiation factor 6 (eIF6) from maturing 60S ribosomal subunits in the cytoplasm. To understand the specific role of SBDS in this process, we solved a high-resolution NMR solution structure of the 29 kDa human SBDS protein, revealing a conserved three-domain architecture. Backbone relaxation measurements demonstrated a conserved global domain motion in which domain I tumbles largely, but not completely, independently of domains II and III. Taken together with complementary genetic and biochemical studies, our data support a model in which SBDS tightly couples the energy of GTP hydrolysis by EFL1 to the dissociation of eIF6 through a conformational coupling mechanism.

TOA 9:20-9:35 High Resolution Structure of a Large Membrane Protein

by Joint X-ray/NMR Calculations and Paramagnetic Relaxation Sensitivity Enhancement

Ming Tang1; Deborah Berthold1; Lindsay J Sperling1; Charles Schwieters2; Anna Nesbitt1; Andrew J. Nieuwkoop1; Robert Gennis1; Chad Rienstra1; 1University of Illinois at Urbana-

Champaign, Urbana, IL; 2National Institutes of Health, Bethesda, MD

Membrane proteins play an important role in most biological processes, such as immune recognition, signal and energy transduction and ion conduction. However, the structure elucidations of membrane proteins are hindered by poor resolution of X-ray data and low sensitivity of NMR spectroscopy. To overcome these challenges, we have demonstrated joint structure calculations with both X-ray and solid-state NMR data to greatly improve the quality for membrane protein structures, and sensitivity enhancement by chelator lipids with paramagnetic metal ions for solid-state NMR of large membrane proteins. These advancements will greatly facilitate the structural studies of complex membrane protein systems.

TOA 9:35-9:50 Compressed Sensing Reconstruction of Undersampled

NOESY Spectra: Application to Large Membrane Proteins Mark Bostock1; Daniel Holland2; Daniel Nietlispach1;

1Department of Biochemistry, University of Cambridge, United Kingdom; 2Magnetic Resonance Research Centre, University

of Cambridge, United Kingdom Multidimensional experiments result in long recording times since Fourier Transformation (FT) requires sampling of the full Nyquist-Shannon grid. Undersampling the time-domain, combined with non-FT processing, can speed up data acquisition. Various introduced approaches work well provided peak intensities are within a small range, e.g. backbone experiments. However, these methods typically fail with NOESY experiments, where the non-linearity of most reconstruction procedures is unable to recover peaks over the large dynamic range of the data. We and others recently showed the use of compressed sensing (CS) as a processing method. Here we demonstrate high quality CS reconstruction of undersampled NOE data, allowing fast acquisition of 3D NOESY experiments on a large membrane protein. Different algorithms and sampling schemes are investigated.

TOA 9:50-10:05

NMR Detection of Redox Reactions in Cu2+-Bound Amyloid-β Fibrils and Resolution Enhanced Solid-State

NMR by SAIL and Ultra Fast MAS Sudhakar Parthasarathy1; Yusuke Nishiyama2; Yuki Endo2;

Takahiro Nemoto2; Masatsune Kainosho3, 4; Yoshitaka Ishii1; 1Univ. of Illinois at chicago, Chicago, IL; 2JEOL Ltd., Tokyo,

Japan; 3Graduate School of Science, Nagoya University, Nagoya, Japan; 4Center of Priority Areas, Tokyo Metropolitan

Univ, Tokyo, Japan In this presentation, we will report two separate topics on solid-state NMR (SSNMR) application and methodology. In the first topic, we examine the redox reactions of Cu2+ ions bound to amyloid fibers of 40-residue amyloid β (Aβ(1-40))and the resultant production of reactive oxygen species (ROS) by 13C and 1H SSNMR and other techniques. In the second topic, we discuss resolution enhancement in 1H and 13C SSNMR by use of SAIL labeled samples under ultra fast magic angle spinning (MAS) conditions (70kHz) in a high magnetic field (1H frequency: vH = 800 MHz). 1H resolution improves by a factor of ~3 by ultra fast MAS at 70 kHz for the SAIL-Isoleucine over the previous studies for SAIL- Valine at MAS 27kHz.

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10:45 am – 1:00 pm, TUESDAY MORNING TUTORIAL SESSION Sanji Han, presiding

Versailles TOB 10:45-11:20 ABC's of NUS

Jeffrey C. Hoch; Univ of Connecticut Health Ctr, Farmington, CT

This tutorial will explore the fundamentals of sampling in one and multiple dimensions, uniform and nonuniform. Nonuniform sampling (NUS) enables high resolution in multidimensional NMR without imposing the time cost of uniformly sampling to long indirect evolution times. Various NUS approaches and non-Fourier methods of spectrum analysis suitable for NUS will be compared and contrasted, and the benefits of NUS will be demonstrated.

TOB 11:20-12:25

Design, Care and Feeding of NMR Probes: A Tutorial Part II

Kurt Zilm; Yale University, New Haven, CT During the second part of this tutorial I will introduce intermediate radio frequency electronics concepts needed to understand the inner workings of NMR probes. Depending on the application, different competing requirements nearly always force the probe designer to compromise some aspect of the performance. Whether you are building, modifying or buying a new NMR probe, an understanding of probe design will help you recognize the compromises important to you, and help the typical user better understand how to properly care for their probe.

TOB 12:25-1:00

Ultrafast Multidimensional NMR – A Coherent Picture? Lucio Frydman; Weizmann Institute, Rehovot, Israel

This tutorial presents a description of experiments for collecting arbitrary multidimensional NMR data sets within a single scan. Attention will be paid to graphical depictions of the main components employed by these “ultrafast” experiments –field gradients, frequency-swept pulses, echoes of various sorts; the relation between variables as known in traditional 2D NMR –spectral widths, resolution, line shapes– and the timing / gradient parameters involved in their single-scan counterparts; and a summary of how to program the spatial and RF manipulations needed for the execution and the special data processing needed by this kind of acquisitions. Should time permit and internet connections available, demonstrations of basic homo- and hetero-nuclear single-scan 2D acquisitions will be assayed/

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10:45 am – 12:20 pm, TUESDAY MORNING MATERIALS

Lyndon Emsley, presiding Trianon

TOC 10:45-11:10 The Benefits and Curses of Ultrabroad NMR Signals:

Methodological Advancements and Scientific Insights from Solid-State 195Pt NMR

Brad Chmelka; University of California, Santa Barbara, Santa Barbara, CA

Intrinsically broad NMR signals reflect the high sensitivities of nuclei to their local environments. While such signals can in principle provide detailed information on associated molecular compositions, structures, and interactions, they are often challenging to excite and detect, especially when lineshapes approach megahertz in width. Recent advancements in the excitation and detection of ultrabroad NMR signals present new opportunities for probing previously intractable solid-state materials. These include heterogeneous solids containing nuclei with extremely large shift ranges, such as 195Pt, that are often of high technological importance. Recent methodological progress will be discussed for excitation and detection of ultrabroad NMR signals, with examples presented for solid-state 195Pt NMR measurements of bulk and nanoscale platinum-containing compounds with complicated molecular order or heterogeneity.

TOC 11:10-11:35

Insights into Radiation Damage and Nuclear Materials from High-Resolution Radiological Nuclear Magnetic

Resonance Ian Farnan; University of Cambridge, Cambridge, United

Kingdom In order to obtain high-resolution solid-state NMR spectra of nuclear materials there are non-trivial safety issues that need to be controlled. Two complementary protocols for the safe operation of a radiological magic angle spinning will be presented. The first involves multiple levels of sample containment within the rotor that operates at modest spinning speeds. A second approach that involves containment of the entire MASNMR probe allows very rapid spinning. Once implemented these techniques open up the field of nuclear materials to new insights ranging from quantitative measures of atomic displacements due to radiation damage to the details of actinide distributions at the atomic scale in nuclear fuel and the interactions and bonding of 5f electron systems.

TOC 11:35-11:50

High Resolution Stray Field Imaging Probe for in situ Battery Studies

Joel A Tang1; Guiming Zhong2; Jason Kitchen1; Peter L. Gor'kov1; Riqiang Fu1; 1National High Magnetic Field

Laboratory, Tallahassee, FL; 2Xiamen Univeristy, Xiamen, PR China

Stray field imaging (STRAFI) provides an alternative imaging method to study Lithium-ion battery electrode materials. Examining the Li-ion exchange within the battery during the charge-discharge process will provide additional information towards advancements of the material’s properties and lifetime. Here we present a high resolution STRAFI probe with in situ charge-discharge capabilities that is used on a 19.6T superconducting magnet with a gradient strength of 86T/m in the fringe field. We demonstrate the ability to

acquire images that can clearly resolve items that are micrometers thick.

TOC 11:50-12:05

Ion Clustering and Transport in Organic Electrolytes: New Insights from PFG NMR

Jianbo Hou; Zhiyang Zhang; Mark D Lingwood; Bryce E Kidd; Louis A Madsen; Virginia Tech, Blacksburg, VA

How do subtle ionic associations affect transport in electrolytes such as ionic liquids (ILs) and conducting polymers? In order to understand such correlations, we must have detailed and quantitative information about the transport of cationic and anionic species as well as neutrals such as water. NMR uniquely provides chemical specificity and experimental flexibility in probing motions of separate species. Thus, our group is using diffusometry and electrophoretic NMR to fundamentally understand ionic conduction mechanisms. We will present observations of the predominance of negative triple ions (- + -) in dry IL electrolytes, which correlate well with complex bending motions in IL-polymer “artificial muscle” mechanical actuators, and promise informed design for next generation batteries, electromechanical devices, and separations applications.

TOC 12:05-12:20

A Large Sample Volume Magic Angle Spinning Nuclear Magnetic Resonance Probe for In-Situ Investigations with

Constant Flow of Reactants Jian Zhi Hu; Jesse A Sears; Hardeep Mehta; Joseph Ford; Ja

Hun Kwak; Kake Zhu; Yong Wang; Jun Liu; David W Hoyt; Mary Hu; Ju Feng; Charles H. F. Peden; Pacific Northwest

National Laboratory, Richland, WA A constant-flow magic angle sample spinning (CF-MAS) NMR probe is reported for in-situ studies of the reaction dynamics, stable intermediates states, and mechanisms of catalytic reactions. In our approach, the reactants are introduced into the catalyst bed using a fixed tube at one end of the MAS rotor while a second fixed tube, linked to a vacuum pump, is attached at the other end of the rotor. The pressure difference between both ends of the catalyst bed inside the sample cell forces the reactants flowing through the catalyst bed, which improves the diffusion of the reactants and products. This design allows the use of a large sample volume for enhanced sensitivity, permitting in-situ 13C CF-MAS studies at natural abundance.

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4:00 – 5:50 pm, TUESDAY AFTERNOON DYNAMICS

Rafael Bruschweiler, presiding Versailles

TOD 4:00-4:25 Ligand Binding and Helix Interactions in GPCR Activation

Steven Smith; Stony Brook University, Stony Brook, NY G protein-coupled receptors (GPCRs) are a large superfamily of membrane receptors that have seven transmembrane helices and respond to a wide array of signaling ligands. Similarities in the sequences of these receptors have led to the idea that they share a common activation mechanism. In contrast, sequence diversity between receptors has been correlated with their specificity for different ligands. I will present recent results on GPCRs from three different subfamilies: rhodopsin from the visual receptor subfamily, the beta2-adrenergic receptor from the amine receptor subfamily and CCR5 from the peptide receptor subfamily. The structural changes within these three GPCRs provide a framework for understanding how GPCRs are activated.

TOD 4:25-4:50

NMR and Molecular Dynamics Simulations: A Perfect Match?

Kresten Lindorff-Larsen; Department of Biology, University of Copenhagen, Copenhagen, Denmark

Long and accurate molecular dynamics simulations have the potential to provide an atomic-level description of the structure and dynamics of biomacromolecules. Recent years have seen dramatic advances in both the timescales accessible to molecular dynamics simulations (now up to the millisecond-timescale) and in the quality of the force fields used in such simulations. NMR spectroscopy has played a central role in the improvement of force fields by providing a wealth of experimental data reporting on a broad range of structural and dynamical properties of peptides and proteins. With a long and accurate simulation in hand, it is in turn possible to provide a structure-based description on the properties probed by NMR experiments in both folded and unfolded proteins.

TOD 4:50-5:05

Analysis Pipeline for Simultaneous Study of Structure and Dynamics of Challenging Proteins from Residual

Dipolar Couplings Stephanie Irausquin; Christopher Schmidt; Mikhail Simin;

Homayoun Valafar; University of South Carolina, Columbia, SC

Studies further contributing to our understanding of protein structure-function relationships have indicated a need for investigations conducted in physiologically relevant timescales and environments. Residual Dipolar Couplings (RDCs) have been recognized as a possible data-source for probing the structure and dynamics of proteins on timescales ranging from pico to microseconds, when most biological functions occur. Despite their promise, little success has been demonstrated due to challenges presented during separation of structural and motional information. Here we present a pipeline, comprised of a number of software tools specifically designed to address different aspects of RDC data extraction and analysis, utilizing a protein which undergoes conformational switching. Our method combines Bioinformatic tools with computational biology approaches and is applicable to other challenging proteins.

TOD 5:05-5:20 Dynamics of the equine Infectious Anemia Virus Capsid Protein: Structural and Functional Implications for the

Conserved β-Hairpin Kang Chen1; Grzegorz Piszczek1; Carol Carter2; Nico

Tjandra1; 1National Institutes of Health, Bethesda, MD; 2State University of New York Stony Brook, Stony Brook, NY

The retroviral capsid (CA) consists of dual-domain (CAN/C) proteins. The proteolytically refolded N-terminal β-hairpin of HIV-1-CA is highly conserved and essential for functional capsid assembly; however, the mechanism remains elusive. The full-length CA protein of EIAV, a lentivirus similar to HIV-1, was deuterated and purified. The weak inter-molecular affinity of EIAV-CA allows backbone resonances assignments, RDC, and spin relaxation measurements. NMR structural data demonstrated that the folded β-hairpin induced helical transitions at conserved residues N-terminal to helix α1, crucial to initiate proper hexamerization of domain CAN. Additional relaxation data indicated the CAN hexamerization and the CAC dimerization occurring independently at sub-ms and ns-µs time scales, respectively. Thus, the rate-limiting capsid assembly step is the hexamerization induced by the β-hairpin formation.

TOD 5:20-5:35 Model of Large Scale Conformation Mobility in Proteins

Yaroslav Ryabov1; G. Marius Clore2; Charles D. Schwieters1; 1DCB, CIT, NIH, Bethesda, MD; 2NIDDK, NIH, Bethesda, MD

We present a general formalism for the computation of orientation correlation functions involving a molecular system undergoing rotational diffusion in the presence of transitions between discrete conformational states. In this formalism there are no proscriptions on the timescales of conformational rearrangement relative to that for rotational diffusion and the rotational diffusion tensors of the different states can be completely arbitrary. Although closed form results are limited to the frequency domain, this is generally useful for many spectroscopic observables as the result allows the computation of the spectral density function. We specialize the results for the computation of the frequency-domain correlation function associated with NMR relaxation.

TOD 5:35-5:50

Expanding Limits of Relaxation Dispersion: Combined Bayesian CPMG, R1rho, and Lineshape Analysis of Low-

Populated, Fast-Exchanging Protein States Lukas Zidek1; Petr Padrta1; Pavel Kaderavek1; Mikael Akke2; Carl Diehl2; Hana Sanderova3; Veronika Papouskova1; Libor Krasny3; Vladimir Sklenar1; 1Masaryk University, Brno, Czech

Republic; 2Lund University, Lund, Sweden; 3Academy of Sciences of the Czech Republic, Prague, Czech Republic

Relaxation dispersion has recently become a useful tool for characterizing "invisible" excited states of proteins. However, the routinely used approaches are limited by the population of the minor state and its exchange rate with the ground state. Low populations and/or interconversion rate outside the favourable timescale results in correlation of the obtained exchange parameters. We present a solution of the problem by combining CPMG and R1rho data and analyzing all points forming the cross-peaks instead of fitting just the peak heights (or volumes). The peaks cut from the spectra measured at two magnetic fields were directly analyzed using Bayesian statistics in the all-at-once manner. The presented application

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documents that apparently insignificant exchange data may have a high biological relevance.

4:00 – 5:50 pm, TUESDAY AFTERNOON

MRI DEVELOPMENTS Michael Garwood, presiding

Trianon TOE 4:00-4:25

New Concepts for Spatial Encoding Jürgen Hennig; University Hospital Freiburg, Freiburg,

Germany In order to overcome physiological limits for gradient switching and to allow more flexible, anisotropic spatial encoding we have introduced non-bijective. multipolar spatial encoding fields (NBSEMs), which allow non-isotropic spatial encoding at very high slew rates. For human use encoding fields using second order cylindrical harmonics for head imaging as well as a one sided- whole body gradient coil have been realized. This PatLoc (parallel imaging technique using localized gradients)-approach can be combined with highly parallel imaging using highly integrated multicoil arrays to speed up data acquisition considerably beyond limitations of conventional MRI. For functional studies acquisition speed of 10 fps and more for a 64x64x64 brain volume have been realized and used to investigate the dynamics of brain connectivity.

TOE 4:25-4:50

Maximum Multiplexing and Parallelization for Encoding with Detectors in MRI

Larry Wald; MGH NMR Core at Martinos Center, Charlestown, MA

This talk will review our experience with highly parallel detection with MR array coils of up to 128 channels in the heart and brain, as well as the alterations in gradient encoding strategy which allow maximum use of the array’s spatial encoding ability. I will discuss the theoretical limits to this approach and show practical implementations in which more than 90% of the encoding derives from the array to, for example, achieve whole-brain single-shot Echo Volume Imaging (EVI) of the head at 3.5mm resolution and 20 frames per second and Simultaneous MultiSlice (SMS) acquisitions at 50 slices per second.

TOE 4:50-5:05

Tracking Dopamine-induced Manganese Transport in the Nervous System of Aplysia californica with MEMRI

Ileana Jelescu1; Romuald Nargeot2; Denis Le Bihan1; Luisa Ciobanu1; 1CEA/DSV/I2BM/Neurospin, Paris, France;

2Université Bordeaux, Bordeaux, France Despite the increased use of manganese as a neuronal tract tracer in preclinical applications the transport mechanism of the ion is not fully understood. Aplysia californica provides an ideal network of identified and large neurons to explore this matter. We performed high resolution manganese enhanced magnetic resonance imaging (MEMRI) on isolated Aplysia buccal ganglia to study the Mn2+ transport in resting state and following dopamine (DA)-induced activation. We confirmed, for the first time using MEMRI, the known axonal projections of identified motor neurons in the peripheral nerves of the ganglia. Images following DA perfusion showed significant modifications in the manganese distribution, reflecting functional changes in the neuronal network.

TOE 5:05-5:20 Modifying Doxorubicin Nano-carriers to Create CEST MRI

Contrast and Subsequent Use for Monitoring Cervical Tumor Therapy

Kannie Chan2; Tao Yu2; Guanshu Liu1; Ming Yang2; Assaf Gilad2; Peter Van Zijl2; Jeff Bulte3; Justin Hanes2; Michael T. Mcmahon1; 1Johns Hopkins University SOM/KKI, Baltimore,

MD; 2Johns Hopkins University School of Medicine, Baltimore, MD; 3Johns Hopkins University, Baltimore, MD

Nanoparticle-based drug treatment has potential for chemotherapy for cervical tumors, but there are hurdles for effective delivery. Recent development in particles with poly(ethylene) glycol (PEG) can overcome these barriers but there is a need for real time in vivo imaging of the particle delivery to monitor therapeutic efficacy. We are interested in using Chemical Exchange Saturation Transfer (CEST), a molecular MRI contrast mechanism, to monitor the vaginal delivery of this pegylated particles to treat local cervical tumors by co-encapsulating CEST contrast agents and drugs within liposomes. The goal is to image the distribution of these particles and to indirectly assess the retention of drugs over the course of treatment.

TOE 5:20-5:35

Generating MRI Contrasts in Rotating Frames of Rank 1≤n≤5 in the Human Brain at 4T and Mouse Brain at 7T Timo Liimatainen1; Silvia Mangia2; Hanne Hakkarainen1;

Andrew Tyan2; Djaudat Idiyatullin2; Dennis Sorce2; Michael Garwood2; Shalom Michaeli2; 1University of Eastern Finland,

Kuopio, Finland; 2CMRR, University of Minnesota, Minneapolis, MN

Here we apply a class of RF pulses that are amplitude and frequency modulated based on recursive functions sine and cosine. The unique feature of these frequency-swept pulses is their ability to generate relaxation-based MRI contrast exploiting rotating frames of rank 1 ≤ n ≤ 5. The method is an extension of the previously introduced technique called RAFF (Relaxations Along a Fictitious Field). The RAFFn method provides reduced SAR as compared to conventional and adiabatic rotating frame methods. By using RAFFn RF pulses, we measured rotating frame relaxation times in human brain at 4 T and mouse brain at 7 T. The highest contrast between grey and white matter in human was obtained when n of RAFF experiment was 4.

TOE 5:35-5:50

Early Detection of Pancreatic Cancers & Brain Tumors by Active Feedback Magnetic Resonance

Zhao Li1; Ryan Quiroz1; Raymond Ngo1; Chaohsiung Hsu2; Yu-Hao Chen2; Clifton Shen3; Mark Girgis4; Hongxiang Hui4;

Vay Go5; Yung-Ya Lin1; 1Department of Chemistry & Biochemistry, UCLA, Los Angeles, CA; 2Department of

Chemistry, National Taiwan Universit, Taipei, Taiwan; 3Crump Molecular Imaging Institute, UCLA, Los Angeles, CA;

4Department of Surgery, UCLA, Los Angeles, CA; 5Center for Excellence in Pancreatic Diseases, UCLA, Los Angeles, CA

Early detection of high-grade malignancy using enhanced MRI techniques significantly increases not only the treatment options available, but also the patients’ survival rate. For this purpose, a conceptually new approach, termed “Active Feedback MR”, was developed. An active feedback electronic device was homebuilt to implement active-feedback pulse sequences for spin avalanching amplification. With this new approach, early detection of pancreatic cancers can be

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achieved through sensitively imaging the dipolar fields induced by targeted magnetic nanoparticles. Early detection of orthotopic glioblastoma multiforme with 4-5 times improved contrast than conventional images can be reached through sensitively imaging susceptibility variations due to irregular water contents and deoxyhemoglobin.

8:30 – 10:05 am, WEDNESDAY MORNING RESOLUTION AND SENSITIVITY

Eriks Kupce, presiding Versailles

WOA 8:30-8:55 Controlled Singlet to Triplet Conversion allows Para

Hydrogen Induced Polarization in Symmetric Molecules Hans W. Spiess; María Belén Franzoni; Lisandro Buljubasich; Kerstin Muennemann; Max Planck Institute Polymers, Mainz,

Germany The problem of low sensitivity in NMR can be overcome by hyperpolarization techniques. This approach is restricted to relatively short time scales depending on the nuclear T1 relaxation times. However, long-lived NMR states like singlet states can be used to store the created hyperpolarization. Parahydrogen Induced Polarization (PHIP) is particularly well suited for the generation of hyperpolarized long-lived states because para-H2 possesses singlet symmetry. In most PHIP experiments the initial singlet state is directly converted to an NMR observable triplet state. Here, we demonstrate the storage of the enhanced PHIP signal as a singlet state in high magnetic fields and its conversion into observable magnetization without chemically altering the spin system.

WOA 8:55-9:20

Ultra High-Resolution NMR in Inhomogeneous Magnetic Fields: Two-Dimensional Long-Lived Coherence

Correlation Spectroscopy Aurélien Bornet1; Srinivas Chinthalapalli2; Takuya Segawa1; Riddhiman Sarkar3; Sami Jannin1; Geoffrey Bodenhausen1;

1Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland; 2Indian Institute of Technology, New Delhi, India;

3University of Southampton, Southampton, United Kingdom Long-lived coherences (LLC’s) involving homonuclear pairs of chemically inequivalent spins can be excited and sustained during protracted radio-frequency irradiation periods that alternate with brief windows for signal observation. Fourier transformation of the sustained induction decays recorded in a single scan yields NMR spectra with line-widths in the range 10 < δν < 100 mHz. We designed a method to excite and detect LLC’s in a broadband manner, allowing one to record two-dimensional NMR spectra that reveal differences of chemical shifts in the indirectly detected dimension and scalar couplings in the directly detected dimension. The line-widths δν can be on the order of 0.5 Hz, even if the homogeneity of the magnetic field is deliberately degraded to δB0/B0 = 10 ppm.

WOA 9:20-9:35 Hyperpolarized Singlet State NMR

Giuseppe Pileio1; Lynda J. Brown1; Michael Tayler1; Christoffer Laustsen2, 3; Richard C. D. Brown1; Jan Henrik

Ardenkjaer-Larsen2, 4; Malcolm Levitt1; 1University of Southampton, Southampton, UK; 2The Technical University of Denmark, Lyngby, DK; 3Aarhus University, Aarhus, DK; 4GE

Healthcare, Broendby, DK Hyperpolarized Singlet State NMR combines sensitivity enhancement provided by dissolution-DNP with the extended lifetime of singlet states. It involves hyperpolarization being deposited into a long-lived state that acts as a reservoir of hyperpolarization from where the user can withdraw at will. Nearly-equivalent spin pairs and ad-hoc developed pulse schemes assure the deposit/retrieval of hyperpolarization and its long-time storage, irrespectively of the magnetic field strength. The 7 minutes lifetime of the singlet state of 15N2O in human blood, or the 10 minutes lifetime of singlet states in some 13C doubly labelled molecules, stimulate speculations on the possible applications of this technique especially in MRI, where prolonged observation of metabolites and other substances, and high contrast/signal-to-noise ratio images are anticipated.

WOA 9:35-9:50 Fast Reconstruction of 0.8% Non-Uniformly Sampled 4D

Methyl-Methyl NOESY by Iterative Soft Thresholding Sven G. Hyberts; Alexander G. Milbradt; Gerhard Wagner;

Dept. Biol. Chem. & Mol. Pharmacologie, Boston, MA The simplicity of the Iterative Soft Thresholding (IST) algorithm currently allows reconstruction of high-resolution 4D methyl-methyl HC-NOESY-HC experiments within a few hours on a 128 CPU cluster. We show the feasibility of this approach on a 0.9 mM ILV labeled sample of the B1 domain of protein G (GB1). The sampling of the three indirect dimensions was determined by a 3D-woven Poisson Gap schedule, which generated 87,248 coordinates in a 60x150x150 hypercomplex grid (1,350,000 points), yielding a sampling density of 0.8%. The result shows that it is feasible to sample up to 1.2 times the relaxation time in all the indirect dimensions of a 4D spectrum for superb resolution

WOA 9:50-10:05

Helium-Cooling and -Spinning Dynamic Nuclear Polarization-Enhanced Solid-State NMR at 14 T and 30 K Yoh Matsuki1; Keisuke Ueda1; Toshitaka Idehara2; Ryosuke Ikeda2; Kosuke Kosuga2; Isamu Ogawa2; Shinji Nakamura3; Mitsuru Toda3; Takahiro Anai3; Toshimichi Fujiwara1; 1Osaka University, Suita, Japan; 2University of Fukui, Fukui, Japan;

3JEOL Resonance Inc, Tokyo, Japan Sensitivity enhancement of solid-state NNR (SSNMR) in the order of 100 is becoming routine via dynamic nuclear polarization (DNP) at T > 90K, B0 < 9.4T, using microwave of frequency νmw < 264GHz. DNP-SSNMR at higher field conditions is challenging because high-power microwave sources at very high frequencies are not commercially available, and because the efficiency of the cross effect-based DNP linearly decreases with the field strength. Here, we report on DNP-SSNMR experiments at one of the highest external field condition B0 = 14.1T, in which we used cold helium gas for cooling and spinning the sample. We observed the DNP enhancement factor of ~23 and ~47 for a static and spinning sample, respectively, at T ~30K.

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10:45 am – 12:20 pm, WEDNESDAY MORNING SMALL MOLECULES Yulan Wang, presiding

Versailles WOB 10:45-11:10

FAST-NMR: Functional Annotation Using Chemical Probes

Robert Powers; University of Nebraska-Lincoln, Lincoln, NE Functional Annotation Screening Technology by NMR (FAST-NMR) is a key component of a diseased-centered systems biology approach to drug discovery. FAST-NMR is based on the premise that proteins with the same function bind a similar set of small molecules. FAST-NMR uses NMR ligand-affinity screens, structural biology and bioinformatics to identify new therapeutic targets. FAST-NMR has been sucessfuly applied to explore the function of a few dozen proteins, including human proteins associated with pancreatic cancer. Recent enhancements to FAST-NMR include functional assignments independent of sequence and structure, the incorporation of in silico screening, enhancements to our CPASS database including interfacing to our new PROFESS database, and the application of NMR-based metabolomics to monitor the in vivo activity of chemical leads.

WOB 11:10-11:35

Fermentanomics: Using NMR Spectroscopy to Improve Cell Culture Performance.

Scott Bradley; Anli Ouyang; Jennifer Purdie; Tim Smitka; Tongtong Wang; Andreas Kaerner; Eli Lilly and Company,

Indianapolis, IN As the number of therapeutic proteins produced by mammalian cell cultures in the pharmaceutical industry continues to increase, the need to improve productivity and ensure consistent product quality during process development activities becomes more significant. To better understand the cellular processes and rationally design media, we have developed a technique for using 1D 1H NMR to rapidly quantitate non-protein feed components and metabolites in the extracellular milieu of mammalian cell cultures. The method, which we call "fermentanomics", was found to generate spectra with excellent water suppression, signal-to-noise, and resolution. Over 50 media components have been identified and are routinely quantitated. In this presentation, we will describe the methodology for analyzing the media as well as present several case studies.

WOB 11:35-11:50

Progress in Spin-Diffusion-Guided Structure Determination of Complexes of Small Molecules and

Large Targets using INPHARMA, STD, tr-NOE, Chemical Shifts and DNP

Marcel Reese1, 7; Victor Sánchez-Pedregal1; Jens Meiler2; Marcel Blommers3; Youngbok Lee6; Karel Kubicek1; Haifeng

Zeng6; Melanie Wegstroth1; Donghan Lee1; Adam Mazur1; Jens Pilger1; Peter Monecke4; Stefan Bartoschek4;

Alexander Schiffer4; Ulrich Wendt4; Stefan Becker1; Christian Hilty6; Teresa Carlomagno5; Christian Griesinger1; 1Max

Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Vanderbilt University, Nashville, TN; 3Novartis Institutes for BioMedical Research, Basel, Switzerland;

4Sanofi-Aventis Deutschland GmbH, Frankfurt am Main, Germany; 5EMBL Heidelberg, Heidelberg, Germany; 6Center

for Biological NMR, College Station, TX; 7Massachusetts Institute of Technology, Cambridge, MA

Better understanding the structure of complexes of weakly binding, small ligands and large macromolecular targets is crucial in the context of improving pharmaceutical lead compounds to become more specific and effective drugs. In this context, firstly, a new analytical-gradient-based refinement method will be presented to use INPHARMA and transferred NOE spectra in XPLOR-NIH driving minimization and simulated annealing protocols. Secondly, it will be shown that using INPHARMA together with STD and tr-NOE creates a new, more robust approach. This will be demonstrated on PKA and a GPCR. Thirdly, complementary DNP-hyperpolarized dual-ligand single-receptor experiments are presented utilizing single scan experiments. Finally, binding modes of weak and strong binding are compared by chemical shift simulation on the tubulin-epothilone system.

WOB 11:50-12:05

Avoiding Strong Coupling Effects in 1JCH Measurements Bingwu Yu; Daron Freedberg; CBER/FDA, Bethesda, MD

Strong coupling can lead to erratic J coupling values for carbohydrates, nucleic acid and some protein side chains. Here we present a new J-modulation method, Constant-Time INEPT HSQC (CTI-HSQC), to accurately measure 1JCH without strong coupling interference, where peak intensity is monitored during an INEPT delay where the total time is held constant and independent of 3JHH evolution. We tested this method on N-acetyl-glucosamine and mannose. Good agreement is achieved between 1JCH measured by this method and previously published simulation data. We further find strong coupling can lead to an error up to 100% for one bond RDCs using coupled HSQC in mannose. We demonstrate that accurate RDCs can also be obtained by CTI-HSQC in the presence of strong coupling.

WOB 12:05-12:20

Chemical Shift Modulations from Fully Refocused Spin-Echo Sequences: the Selective Dynamical Recoupling

Experiment Pieter Ernst Scholtz Smith1; Guy Bensky1; Gonzalo Agustin

Alvarez2; Gershon Kurizki1; Lucio Frydman1; 1Weizmann Institute of Science, Rehovot, Israel; 2Dortmund University,

Dortmund, Germany Since the pioneering works of Carr-Purcell and Meiboom-Gill, π-pulse trains have featured amongst the main tools for controlling spin Hamiltonians. Echo trains find widespread use in NMR and MRI, thanks to their ability to free the evolution of a spin-1/2 from linear Iz terms, like chemical shifts and inhomogeneity effects. Spin echoes have also been researched in dynamic decoupling scenarios, for prolonging the lifetimes of quantum states or coherences. Inspired by this search we introduce a new family of spin-echo sequences, which although fulfilling <Iz>=0 can still detect site-specific interactions like the chemical shift. This is achieved thanks to the presence of weak environmental fluctuations of common occurrence in high-field NMR –such as homonuclear spin-spin couplings or chemical exchange.

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10:45 am – 12:20 pm, WEDNESDAY MORNING EXOTICA

Dieter Suter, presiding Trianon

WOC 10:45-11:10 Optically Re-Writable Patterns of Nuclear Magnetization

in Gallium Arsenide Jeffrey Reimer; UC Berkeley, Berkeley, CA

We have figured out how to exploit the various electron-nuclear relaxation mechanisms so as to use a simple laser beam to write a pattern of NMR signals in a GaAs wafer. The "we" includes my student Jonathan King, Prof. Carlos Meriles at CUNY, and his student Yunpu Li. In brief, we harness the different dependencies of relaxation mechanisms on donor occupation probability, free electron concentration, and nuclear spin isotope to create patterns of nuclear polarization. We then use high field stray-field NMR imaging to demonstrate all-optical creation of micron scale, re-writable patterns of positive and negative nuclear polarization without the need for ferromagnets, lithographic patterning techniques or pulsed, high-power gradients.

WOC 11:10-11:35

Earth's Field MRI in the Freshman Physics Lab: Hardware, Software and Strategy

Carl A. Michal; University of British Columbia, Vancouver, Canada

We have designed an Earth's Field MRI spectrometer that is inexpensive enough to allow construction of a class-set, 18 complete systems, on a very modest budget. The systems are the basis for a revised laboratory component of an introductory physics course aimed at non-physics students. We plan to leverage the health-sciences related career plans of many of these students to engage their interest in both the equipment and underlying physics. Lab activities guide students to explore electronic circuits, oscillations, magnetic fields, magnetic induction, and resonant circuits in the context of MRI. Performance of the system, considering its cost is outstanding, allowing 2D images to be acquired in about 15 minutes.

WOC 11:35-11:50

SUCCESS: Suppression of Undesired Chemicals using Contrast-Enhancing Singlet States

Stephen Devience1; Ronald Walsworth2, 3; Matthew Rosen4, 5; 1Harvard University Department of Chemistry and Che,

Cambridge, MA; 2Harvard-Smithsonian Center for Astrophysics, Cambridge, MA; 3Harvard University

Department of Physics, Cambridge, MA; 4Harvard Medical School, Boston, MA; 5Martinos Center for Biomedical Imaging,

Boston, MA Nuclear magnetic resonance spectra of complex chemical mixtures often contain unresolved and unseen spectral components that can be uncovered using quantum filtration. We demonstrate a novel method of quantum filtration utilizing the nuclear spin singlet state. We create a singlet state in a target molecule and then apply a continuous RF field to both preserve the singlet and saturate the magnetization from interfering molecules. The transfer of spin polarization to the singlet is highly controllable through pulse sequence parameters, so that spectral contrast can be achieved between molecules with very similar structures. We demonstrate the “SUCCESS” technique for 1H NMR of three

molecules relevant to neuroscience: threonine, aspartate, and glutamine, as well as for 31P NMR of NADH and ADP.

WOC 11:50-12:05

Comprehensive Multiphase NMR Spectroscopy: A Powerful Approach for Natural Samples

Andre J Simpson1; Denis Courtier-Murias1; Ronald Soong1; Hussain Masoom1; Adolfo Botana1; James Longstaffe 1; Hashim Farooq1; Myrna J Simpson1; Werner E. Maas2; Michael Fey2; Brian Andrew2; Jochem Struppe2; Howard

Hutchins2; Sridevi Krishnamurthy2; Rajeev Kumar3; Martine Monette3; Henry J. Stronks3; Alan Hume3; 1University of

Toronto, Scarborough, ON; 2Bruker Biospin, Billerica, MA; 3Bruker BioSpin Canada, Milton, ON

Heterogeneous samples, such as soils, sediments, plants, tissues, foods and organisms, often contain liquid-, gel- and solid-like phases. Drying, extracting and fractionating samples can potentially remove important structural information. Here a Comprehensive Multiphase-Nuclear Magnetic Resonance (CMP-NMR) probe is introduced that permits all bonds in all phases to be studied and differentiated in whole unaltered natural samples. The CMP-NMR probe is built with high power circuitry, Magic Angle Spinning (MAS), is fitted with a lock channel, pulse field gradients, and is fully susceptibility matched. Consequently, this novel NMR probe can cover all HR-MAS aspects without compromising power handling thus permitting the full range of solution-, gel-and solid-state experiments available today.

WOC 12:05-12:20

Solid State NMR at Cryogenic Temperature Maria Concistre1; Ole G. Johannessen1; Salvatore Mamone1; Riddhiman Sarkar1; Elisa Carignani2; Mark Denning1; Yasujiro

Murata3; Judy Y. Chen4; Nicholas J. Turro4; Marina Carravetta1; Philip T. Williamson1; Marco Geppi2; Maithan K.

Al-Mosawi1; Carlo Beduz1; Yifeng Yang1; Malcolm Levitt1; 1University of Southampton, Southampton, United Kingdom;

2University of Pisa, Pisa, IT; 3Kyoto University, Kyoto, JP; 4Columbia University, New York, US

We have custom-built a cryogenic NMR equipment able to perform both static and magic-angle-spinning solid-state NMR experiments in a field of 14.1 Tesla. The static cryogenic probe can perform solid state NMR at a temperature down to 1.8 Kelvin while the cryogenic MAS probe can spin a 2 mm zirconia rotor at 15 kHz and 13 Kelvin (true sample temperature). In this contribution we show results for a series of experiments performed in the cryogenic regime under both static and magic-angle-spinning conditions on three systems: endofullerenes, b2-microglobulin (B2M) and Ibuprofen sodium salt where we investigated different and interesting phenomena happening in the cryogenic regime.

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4:00 – 5:50 pm, WEDNESDAY AFTERNOON MOTION AND DYNAMICS J. Patrick Loria, presiding

Versailles WOD 4:00-4:25

RNA-based Regulation Elements Studies by NMR Spectroscopy

Harald Schwalbe1; Jorg Rinnenthal1; Hannah Steinert1; Dominik Wagner1; Anke Reining1; Boris Furtig1; Janina Buck1; Anna Wacker1; Senada Nozinovic1; Thorsten Marquardsen2;

1Univ of Frankfurt, Frankfurt, Germany; 2Bruker Biospin, Rheinstetten, Germany

Recently, the importance of RNA-based regulation has become increasingly recognized. Regulation is based on structural transitions of RNA modules located in the 5' untranslated region of mRNA. The regulation mechanism acts on the level of transcription as well as translation. Riboswitches sense changes in the concentration of small molecule metabolites while RNA thermometers respond to temperature changes. In this contribution, we will describe the detailed characterization of RNA thermometers. We have developed methods to determine individual base pair stabilities of these regulation elements and have developed a T-jump probe to monitor transitions by real-time NMR. Elucidation of the coupling of binding of allosteric structural transitions of the regulation events will be discussed iwth the examples of translational riboswitches.

WOD 4:25-4:50

Ligand-Mediated Conformational Dynamics in the Catalytic Function of the Alpha Subunit of Tryptophan

Synthase David Boehr; Jennifer Axe; Penn State, University Park, PA

The alpha subunit of tryptophan synthase catalyzes the retro-aldol cleavage of the C3’-C3 bond of indole-3-glycerol phosphate (IGP) to indole and D-glyceraldehyde 3-phosphate (G3P). The catalytic mechanism is proposed to involve a single intermediate, an indolenine tautomer, and general acid/base catalysis by the conserved amino acid residues Glu49 and Asp60. TROSY-based 15N R2 relaxation dispersion experiments demonstrate that the internal motions of the enzyme on the µs-ms timescale (i.e. same timescale as catalysis) differ depending on what ligands are bound at the active-site. Intriguingly, new µs-ms timescale dynamics, which are not present in the ligand-free enzyme, are induced in the region around Glu49 when G3P is bound. These motions may thus be tied directly to the catalytic function of tryptophan synthase.

WOD 4:50-5:05

High-Pressure NMR Reveals that the Native State of Proteins Contains the "Dry" Molten Globule

Yinan Fu1; Vignesh Kasinath1; Veronica Moorman1; Nathaniel Nucci1; Vincent Hilser2; Joshua Wand1; 1Univ of Pennsylvania, Philadelphia, PA; 2Johns Hopkins University, Baltimaore, MD

A critical aspect of proteins is their cooperative substructure and internal motion. NMR relaxation is used to monitor the effects of high-pressure on fast motion in ubiquitin. Unlike the main chain, motions of the side chains have a large and variable pressure dependence. Within the core, this pressure sensitivity correlates with the magnitude of motion at ambient pressure. Spatial clustering of the pressure sensitivity is also seen indicating limited cooperativity of motion on the sub-nanosecond time scale and suggesting regions of variable

compressibility.It would seem that the native ensemble contains a significant fraction of members with characteristics ascribed to the “dry molten globule.” The accompanying side chain conformational entropy helps complete our view of the thermodynamic architecture underlying proteins.

WOD 5:05-5:20

Motion of Disordered Protein Studied by PREs, 15N Relaxation, and MD Simulations: How Fast is Segmental

Diffusion in Denatured Ubiquitin? Yi Xue; Nikolai R. Skrynnikov; Purdue University, West

Lafayette, IN Long MD trajectories of disordered ubiquitin (wild-type and MTSL-tagged mutants) have been recorded using a GPU computer. The results of the MD simulations have been used to model 15N relaxation rates, PREs, and radius of gyration, leading to near-quantitative agreement with the experimental data (8M urea, pH 2). Of note, the MD-based approach rigorously predicts the quantities that are inherently dynamic, i.e. dependent on the motional correlation times. The analysis of the PRE data allowed for accurate determination of the segmental diffusion coefficient which characterizes the relative translational motion of the MTSL label and the individual HN atoms, D = 0.5×10-6 cm2/s.

WOD 5:20-5:35

Excited States of the HIV Dimerization Initiation Site RNA Revealed by NMR

Katja Petzold; Hashim Al-Hashimi; University of Michigan, Dept. Biophysics, Ann Arbor, MI

The dimerization initiation site (DIS) is a regulatory RNA of the HIV-virus. Upon viral maturation DIS undergoes dimerization, which is essential for the production of viruses. The mechanism of this secondary structure rearrangement – a complete exchange of strands – remains unknown. We investigated the role of µs- to ms-motions using relaxation-dispersion NMR measurements to reveal possible dimer-forming transition states. We determined the excited state chemical shifts of 9 nucleotides and their corresponding secondary structures, and confirmed those results by mutagenesis. This combined data suggests that the two mutually exclusive excited states exits which might form a bulge-zipping complex, required for DIS-dimerization. Finally, using biochemical experiments, we demonstrated that quenching of these motions reduces dimerization potential.

WOD 5:35-5:50

Electrostatic Interactions and Description of the Encounter Complex in Binding of Proline Rich Motifs to a

SH3 Domain Erick Alejandro Meneses Ramirez; Anthony Mittermaier; McGill University, Department of Chemistry, Montreal,

Canada In this project we have investigated the role of electrostatic interactions in the binding of a Fyn SH3 domain with several proline rich peptides. Three different dodecapeptides containing a proline rich core were selected to bind to a wild-type fyn SH3 domain. NMR and calorimetric results showed that the peptides with the sequences Ac-WSLAXRLPPLP-NH2 interact with the binding pocket on the protein through a conserved Arg-Asp interaction. This interaction accounts for a 30 fold enhancement in the binding constant at infinite salt concentration. Kinetic experiments through NMR have also showed the presence of only short range electrostatic

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interactions at the encounter complex. This suggests the formation and encounter complex with a structure closely similar to that of the bound state.

4:00 – 5:50 pm, WEDNESDAY AFTERNOON

MRI/MRS Daniel Vigneron, presiding

Trianon WOE 4:00-4:25

MR Metabolic Imaging of Cancer Sarah Nelson, UCSF, San Francisco, CA

WOE 4:25-4:50

Revisiting Decades-Old Spin Physics to Improve Modern Magnetic Resonance Imaging

Warren S. Warren; Duke University, Durham, NC We will re-examine a variety of magnetic resonance effects which were assumed to be well characterized decades ago, but which in fact were not completely understood; the consequence is prediction and demonstration of new sources of contrast, and an improved quantitative understanding of imaging effects. We have recently found that the classical (Bloch equation) treatment of dipolar interactions in solution needs to be modified significantly, with very broad applications; for example, matched gradient pulse pairs, a seemingly innocuous module in thousands of sequences, can alter time evolution in unexpected ways. We have also found that unequal pulse spacing in echo sequences can enhance signal, and specific pulse sequences can dramatically extend T1 by accessing long-lived states between equivalent spins.

WOE 4:50-5:05

2D Ultrafast J-resolved MRS Sequence with 3D Localization: an in vitro Validation on a 7T Imaging

System Serge Akoka1; Tangui Roussel2; Patrick Giraudeau1; Hélène

Ratiney2; Sophie Cavassila2; 1CEISAM, UMR 6230, CNRS/Université de Nantes, Nantes, France; 2CREATIS,

UMR 5220, Universite de Lyon, Lyon, France 2D MRS is a well known tool for the analysis of complicated and overlapped MR spectra and was therefore originally used for structural analysis. It also presents a potential for biomedical applications as shown by an increasing number of works related to localized in vivo experiments. However, it suffers from long acquisition times due to the collection of numerous increments in the indirect dimension (t1). This paper presents the first 3D localized 2D ultrafast J-resolved MRS sequence, developed on a small animal imaging system, allowing the acquisition of a 3D localized 2D J-resolved MRS spectrum in a single scan. Sequence parameters were optimized regarding Signal-to-Noise ratio and spectral

WOE 5:05-5:20

Mapping the Phase Diagram for Anomalous Diffusion in the Rat Brain at 17.6 T

Carson Ingo; University of Illinois at Chicago, Chicago, IL Diffusion in biological tissue is anisotropic and has a complex time and length scale dependence. While the diffusion tensor captures directional dependence, multi-exponential models do not fully describe the signal decay. Such anomalous diffusion is an extension of the Gaussian random walk model to fractional-order in space and in time. Here we map the phase space for white and gray matter regions of a fixed rat brain for b-values up to 24,000. For a Stejskal-Tanner pulse sequence

the results were different in different gradient directions, and for variation of mixing time and for gradient strength. The experimental data were fit well by a Mittag-Leffler function. Hence, this model may be of use in identifying a new fractional-order biomarker for diffusion.

WOE 5:20-5:35

Measuring the Permeability and Stability of Microcapsules with Dynamic NMR Microimaging

Stefan Henning1; Daniel Edelhoff1; Benedikt Ernst1; Sabine Leick2; Heinz Rehage2; Dieter Suter1; 1Exp. Physics III, TU Dortmund, Dortmund, Germany; 2Phys. Chemistry II, TU

Dortmund, Dortmund, Germany We present methods for evaluating the applicability of microcapsules used for controlled and site specific delivery of drugs. By quantitative measurements of the time and space dependent concentrations of paramagnetic contrast agents in the capsules with dynamic NMR microimaging and fitting the numerical simulations of the diffusion to the experimental data, we obtained diffusion coefficients in the capsule membranes, which reveal how different preparations decrease their permeability. In addition, we also show how the capsules dissolve in intestinal media whereas they remain stable in gastric media by using a microscopic FLASH sequence for serial acquisition of images.

WOE 5:35-5:50

Ovarian Cancer Detection Using Hyperpolarized 13C-Pyruvate with MR Imaging and Spectroscopy

Mehrdad Pourfathi1; Stephen J. Kadlecek1; Harrila Profka1; Hoora Shaghaghi1; Moses Darpolor1; Kiarash Emami1;

Nicholas N. Kuzma1; Jan H. Ardenkjær-Larsen2; Rahim R. Rizi1; Janet A. Sawicki3; 1University of Pennsylvania,

Philadelphia, PA; 2GE Healthcare, Brøndby, Denmark; 3Lankenau Institute for Medical Research, Wynnewood, PA

Lactate dehydrogenase (LDH) has been shown to be unregulated in ovarian cancer, which may result in elevated lactate concentrations in the tumors. The use of hyperpolarized 13C to highlight lymphoma and prostate tumors using MRSI suggests a utility to detect small, early-stage ovarian tumors. In the analysis performed for this study, we sought to distinguish between (a) elevated levels of LDH activity, causing a more rapid approach to the equilibrium lactate:pyruvate ratio, and (b) a skewing of the ratio itself, due to shifts in the redox state or other factors selectively favoring the forward pyruvate to lactate reaction over the reverse reaction.

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8:30 – 10:05 am, THURSDAY MORNING EXOTICA MRI

Joseph Helpern, presiding Versailles

ThOA 8:30-8:55 Balanced SSFP as a Marker of Magnetic Susceptibility in

the Brain Karla Miller; FMRIB Centre, Oxford , United Kingdom

Steady-state free precession (SSFP) is a fascinating pulse sequence that elicits unusual properties based on steady-state magnetization dynamics. One unique and important property is the signal dependence on resonance frequency. In this talk, I will describe how BSSFP off-resonance properties can be used as a marker for magnetic susceptibility in the brain.

ThOA 8:55-9:20 Nanoscale Spin Imaging

Jorg Wrachtrup; Universitat Stuttgart, Stuttgart, Germany Diamond defect centers provide the opportunity to detect and image spins with single spin sensitivity and nm spatial resolution. When deposited on the tip of an atomic force microscope single defects are capable to detect the spin noise of e.g. electron spins in proteins. At the same time diamond defect can be used to image and detect spins in microfluidic devices with unprecedented sensitivity and resolution. The talk will describe applications and recent advances of diamond spin based EPR and NMR detection.

ThOA 9:20-9:35 Combining Double Quantum Filtering and Magnetization

Transfer with UTE to Obtain Images Based on Macromolecular Characteristics

Uzi Eliav1; Michal Komlosh2; Peter J. Basser2; Gil Navon1; 1Tel Aviv University, Tel Aviv, Israel; 2National Institutes of

Health, Bethesda, MD We propose that intramolecular dipolar interactions in macromolecules (MM) can be probed with MRI by: 1) exciting selectively the MM magnetization, 2) transferring it to water, and 3) obtaining MRIs from the water signal. In the current study the first step is done by double quantum filtered NMR; the second is done with magnetization transfer (DQF-MT). Previous studies left unanswered the role of the water T2 in generating the MM based MRI contrast. Here, we use DQF-MT weighted ultra-short TE (UTE) MRI and demonstrate in spinal cord and rat tail that the source of this new contrast is the amount and structure of the MM within the various tissue compartments.

ThOA 9:35-9:50

In-situ 7Li MRI of Li-ion Batteries S. Chandrashekar1; Nicole Trease2; Hee-Jung Chang2; Alexej

Jerschow1; Clare P. Grey3; 1new york university, New York, NY; 2stony Brook University, Stony brook, NY; 3University of

Cambridge, Cambridge, United Kingdom We conducted "in-situ" 7Li MRI and CSI (at 194.4 MHz) of a symmetric Li metal battery contained in a plastic cell after sequentially charging stages. Progressive Li microstructure formation occurs, which can be seen directly in the images. In 7Li NMR, microstructural Li metal exhibits a distinct chemical shift range relative to the bulk metal. Chemical shift imaging (CSI) further exploits this feature to augment spatial information contained in ordinary MRI images to clearly distinguish Li microstructure formation from bulk Li metal.

ThOA 09:50-10:05

Long Lived Coherent Response Signal: New Echoes and Bone Signals

Boyang Zhang1; Jae-Seung Lee1; Anatoly Khitrin2; Alexej Jerschow1; 1New York University, New York, NY; 2Kent State

University, Kent, OH The Long Lived coherent Response (LLR) signal holds great potential for bone imaging. Experimental results clearly distinguish the LLR signal from a conventional selective excitation method. The LLR echo, a new pulse sequence, is also shown to produce high-sensitivity narrow signals in bone and collagen samples, thereby allowing high-resolution imaging. This new sequence gives stronger intensity and also enables the possibility of slice selection. Together with the LLR signal, the two methods could be combined and optimized for both trabecular and cortical bone imaging, illuminating new ways for in vivo bone imaging.

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10:45 am – 12:20 pm, THURSDAY MORNING SCREENING

Istvan Pelczer, presiding Versailles

ThOB 10:45-11:10 Screening Stress-induced Systems Metabolic Responses

using NMR Huiru Tang; Yulan Wang; Wuhan Institute of Physics and

Mathematics, Wuhan, China Analysis of metabolite composition (metabonome) and its dynamic responses is an important way to unravel the mechanistic aspects of exposomic effects of both biotic and abiotic stressors on plants and animals. The combined NMR-MS techniques and integrated metabonome-transcriptome analysis have become the most effective ways to achieve the metabonome-wide understandings. Here, we will report some recent developments of the combined NMR/MS methods for metabonomic analysis and integrated metabonome-transcriptome approaches with particular aims towards the systems metabolic responses to various exposomic stresses in both plants and animal models. We will discuss the observation of common metabolic reprogramming against oxidative stresses induced by biotic and abiotic stressors. The usefulness and effectiveness of integrated metabonomic analysis will be particularly reflected in this presentation.

ThOB 11:10-11:35

New Insights into Food Quality Control by NMR Based Screening

Manfred Spraul; Hartmut Schaefer; Birk Schuetz; Fang Fang; Eberhard Humpfer; Bruker BioSpin, Rheinstetten, Germany

Only time domain NMR was used for longer time to investigate food material , to look into properties like moisture content or fat content. High Resolution NMR allows the investigation of multiple properties of a food sample with one measurement, such being able to replace several analysis tools, needed to obtain the same information content. This is achieved by the combination of targeted (quantitative) and untargeted analysis. Untargeted Analysis means building normal models for certain product properties and to compare new samples to the normal models available. Such even unknown deviations can be detected, which are NMR visible. Regression analysis allows to further increase the number of parameters detectable by NMR.

ThOB 11:35-11:50

Automating the Processing and Analysis of High Throughput Ligand-Protein Binding Spectra within the

MestReNova System Chen Peng1; Manuel Perez1; Juan Carlos Cobas1; Xiaolu

Zhang2; Jasna Fejzo2; Jaison Jacob2; Andreas Lingel3; 1Mestrelab Research, Santiago de Compostela, Spain;

2Novartis Institutes for BioMedical Research, Inc., Cambridge, MA; 3Novartis Institutes for Biomedical Research, Emeryville,

CA Here we present a software module being developed within the MestReNova software system for streamlining the processing and analysis of high throughput ligand-protein binding spectra, such as STD, T1ρ, and WaterLOGSY. It consists of a group of scripts for batch processing and collating the mixture and library spectra, aligning and normalizing the spectra, picking peaks by deconvoluting the whole spectra and extracting useful spectral parameters, matching library peaks with the mixture ones, and comparing

intensity changes to identify primary hits. The practical aspects and our experiences are discussed on how to optimize such analysis using several real world datasets.

ThOB 11:50-12:05

Metabolomics of Intact Tissues: Discrimination Between Different Regions of Osteolytic Lesions in Multiple

Myeloma Patient using 1H HRMAS NMR spectra Silvia Mari1, 4; Francesca Fontana1; Jose Garcia Manteiga1;

Edoardo Gaude1; Simone Cenci1; Enrico Caneva2; Giovanna Musco1; Stanislav Sykora3; Juan Carlos Cobas Gomez5; 1S.

Raffaele Scientific Institute, Milan, IT; 2Università degli Studi di Milano, Milan, IT; 3Extra Byte, Castano Primo, IT; 4R4R,

Rodano, IT; 5Mestrelab Research, Santiago de Compostela, ES

Multiple myeloma (MM) is a malignancy of plasma cells characterized by multifocal bone lesions and systemic complications due to distant end-organ damage. The metabolic profiling or metabolomics of disease has proven useful to identify diagnostic and prognostic markers. We thus set out to develop the metabolomic study of myeloma-induced bone disease. To this aim, bone tissue biopsies have been collected from MM patients undergoing orthopedic surgery and analyzed by High Resolution – Magic Angle Spinning Nuclear Magnetic Resonance (HR-MAS NMR). Here we present an integrated application based on the R-package MUMA and Mnova software for the processing, analysis and classification of different regions of osteolytic lesions in a MM patient’s bone tissue biopsies.

ThOB 12:05-12:20

Boosting Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States

Nicola Salvi; Aurélien Bornet; Roberto Buratto; Geoffrey Bodenhausen; Ecole Polytechnique Fédérale de Lausanne,

Lausanne, Switzerland A powerful new method for the study of ligand-protein interactions by NMR exploits the unusual lifetimes of long-lived nuclear singlet states. Experimental and theoretical evidence indicates that the new method provides better contrast between bound and free ligands, and hence requires dramatically lower protein concentrations compared to traditional techniques based on longitudinal relaxation of protons (in our examples, 10 rather than 100 mM). Either direct titration of the ligand under investigation or competition experiments can be monitored by LLS relaxation. Furthermore, the method allows fast and inexpensive screening of a library of compounds for drug discovery. We present applications to the screening of potential inhibitors of the urokinase-type plasminogen activator, which is a prototypical target of cancer research.

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10:45 am – 12:20 pm, THURSDAY MORNING SOLIDS II

Marc Baldus, presiding Trianon

ThOC 10:45-11:10 Conformational Exchange Processes in Membrane

Proteins and Enzymes by Solid State NMR Ann Mcdermott; Manasi Bhate; Benjamin J Wylie; Columbia

University, New York, NY The plasticity of ion channels is clearly critical to the many essential processes they carry out in all cells. The simple prokaryotic potassium ion channel, KcsA, has favorable properties for solid state NMR studies. The highly conserved ion-binding selectivity filter of exhibits clearly resolved and site specifically assigned NMR chemical shifts that allowed us to probe site-specific affinities of the ions, and to observe a related slow conformational exchange process. SSNMR methods for characterizing such a millisecond conformational exchange processes with high resolution conditions will be discussed. Based on extensive assignments throughout the protein we also obtain insights into the participation of other residues in the binding process.

ThOC 11:10-11:35

Amyloid Fibril Structures: Methods and Results Wei Qiang; Junxia Lu; Kan-Nian Hu; Wai-Ming Yau; Alexey Potapov; Kent Thurber; Robert Tycko; National Institutes of

Health, Bethesda, MD We have been using solid state NMR methods (plus electron microscopy and other techniques) to investigate the molecular structures of amyloid fibrils since 1998. Our latest results will be described, including the discovery and characterization of a novel antiparallel beta-sheet structure in fibrils formed by a disease-associated mutant of the beta-amyloid peptide, and structural studies of beta-amyloid fibrils derived from brain tissue of Alzheimer's disease patients. Methods that enable this work will also be described, including our Monte Carlo/simulated annealing program for resonance assignments from arbitrary combinations of multidimensional spectra, and quantitative "backbone recoupling" (15N-BARE and 13C-BARE) techniques for obtaining conformational restraints for uniformly labeled samples.

ThOC 11:35-11:50

Solid-State NMR of Viral Particles Emeline Barbet-Massin1; Michele Felletti1; Stefan Jehle1;

Anne Lesage1; Arne Linden2; Sascha Lange2; Trent Franks2; Umit Akbey2; Hartmut Oschkinat2; Kaspars Tars3; Guillaume Communie4; Robert Schneider4; Malene R. Jensen4; Martin Blackledge4; Lyndon Emsley1; Guido Pintacuda1; 1CRMN /

ENS Lyon, Villeurbanne, France; 2FMP Berlin, Berlin, Germany; 3Biomedical Research and Study Center, Riga,

Latvia; 4IBS, Grenoble, France We present solid-state NMR data at a variety of MAS rates, field strengths and temperatures (including 1GHz spectra under 60kHz MAS, and DNP enhanced 400 MHz spectra at 100 K) on viral nucleocapsids from Measles virus (MeV) and Acinetobacter Phage205 (AP205). 13C-13C and 15N-13C correlations and water-edited experiments on MeV were used to monitor the effects of a structural rearrangement following cleavage of the flexible C-terminal portion of the capsid protein. Sensitive J-decoupled 15N-13C and proton-detected 1H-15N fingerprint correlations were recorded on AP205 to provide the basis for backbone resonance assignment.

DNP-enhanced 13C-13C SQ-SQ and DQ-SQ experiments at 100 K are used on both systems to map out the nucleotide spin systems and detect RNA-protein interactions.

ThOC 11:50-12:05

Supramolecular Structure of Membrane-Associated Polypeptides by Combining solid-state NMR and

Molecular Dynamics Simulations Markus Weingarth1; Christian Ader1; Adrien Melquiond1;

Deepak Nand1; Olaf Pongs2; Stefan Becker3; Alexandre M. J. J. Bonvin1; Marc Baldus1; 1Utrecht University, Bijvoet Center,

Utrecht, Netherlands; 2Instut fur Neurale Singnalverabeitung,Univ Hamburg, Hamburg, Germany; 3Max

Planck Insitute for Biophysical Chemistry, Gottingen, Germany

Elemental biological functions such as signal transduction are critically modulated by the dynamic interplay between polypeptides and the membrane environment. Determining such supramolecular arrangements poses a significant challenge for classical structural biology. We introduce an iterative approach that combines MAS ssNMR spectroscopy and atomistic Molecular Dynamics simulations for the determination of supramolecular structure of membrane-bound systems with a resolution and level of accuracy difficult to obtain by either method alone. Our ssNMR-MD joint-approach is demonstrated on the supramolecular structure (comprised of peptide structure & topology and peptide-water/lipid interactions) determination of the membrane-bound Shaker B peptide, that is representative for rapid N-type inactivating domains of voltage gated potassium channels. Furthermore, we show preliminary extensions of our approach to integral membrane proteins.

ThOC 12:05-12:20

Dual Acquisition Magic Angle Spinning (DUMAS) Solid-State NMR: A new Approach to Simultaneous Acquisition

of Multi Dimensional Spectra of Biomacromolecules Gopinath Tata1, 2; Gianluigi Veglia1, 2; 1University of

Minnesota, Minneapolis, MN; 2University of Minnesota, Minneapolis, MN

A new method for dual acquisition of multidimensional MAS (DUMAS) solid-state NMR experiments is presented. The method utilizes a simultaneous Hartmann-Hahn cross polarization from 1H to 13C and 15N and exploit the long-living nature of 15N polarization for parallel acquisition of two multidimensional experiments. The DUMAS approach almost doubles the capability of NMR spectrometers by concatenating various NMR pulse sequences and thus pushing forward the current limits of resolution and sensitivity. DUMAS ssNMR is demonstrated on a microcrystalline ubiquitin and a membrane protein phospholamban. This method does not require any additional hardware and can also be combined with other advancements such as DNP, PRE and perdeuterated sample preparations.

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4:00 – 5:50 pm, THURSDAY AFTERNOON SOFTWARE AND HARDWARE

Frank Engelke, presiding Versailles

ThOD 4:00-4:25 Characterization of Free Energy Landscapes of Proteins

using NMR Spectroscopy Michele Vendruscolo; University of Cambridge, Cambridge,

United Kingdom Abstract: It is becoming increasingly evident that the dynamics of proteins play a crucial role in many of their biological functions, including ligand binding and enzyme catalysis. It is therefore of very great importance to be able to characterize such dynamics at a high level of detail in order to obtain a better understanding of the mechanisms by which proteins perform their activities. I will describe recent advances in the development of procedures to include NMR information about dynamics in the process of protein structure determination, and that provide ensembles of conformations that represent with accuracy the free energy landscapes of proteins.

ThOD 4:25-4:50 Probing Mysteries of NMR Stark Spectroscopy with New

Hardware & Old Software Jim Kempf; Matthew Tarasek; David Goldfarb; Rensselaer

Polytechnic Inst., Troy, NY We developed sequences and hardware to quantify NMR Stark effects at room T and high-field, aiming for methods to map electrostatics. I present two methods for quadrupolar Stark effects (QSEs) using GaAs as a "proving ground". Each utilizes rf E fields at 2�0, a resonant condition allowing quantification of QSEs << solids linewidths. One is a ‘wide-line’ steady state method, the other a high-resolution POWER (Perturbations Observed With Enhanced Resolution) scheme, where few-�s, phase-coherent 2�0 pulses define tensorial QSE response. Results prove theories of orientation-dependent polarization response. Non-AHT lineshapes that currently limit quantitation were explored using GAMMA. That suggests improvements from 2nd averaging, as well as complementary of a similar POWER method using dc E fields.

ThOD 4:50-5:05

High Spin-Lock (> 4 kHz) for R1rho using a Cryogenically Cooled Probe

David Ban1; Alvar Gossert2; Helena Kovacs3; Karin Giller1; Stefan Becker1; Christian Griesinger1; Donghan Lee1; 1Max

Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Novartis Institutes of BioMedical Research, Basel,

Switzerland; 3Bruker BioSpin AG, Fällanden, Switzerland Protein motions that occur in the milli- to microsecond time range are frequently explored by relaxation dispersion experiments. Characterization of microsecond motions requires experiments that are sensitive to this timescale of motions. Through the utilization of a cryogenically cooled NMR probe, we could generate a v1 of 6.4 kHz, which is well above the previous limit of v1, that can be used for the detection of faster motions (~25 µs). This approach was validated by using an on-resonance R1rho experiment that allows for residues that undergo chemical exchange to be modulated only by the RF field. The use of high v1 fields will be of important use to further extend the range of accessible timescales by NMR relaxation dispersion experiments.

ThOD 5:05-5:20 Determination of a High-Resolution Model of the Type-III

Secretion System Needle Using Solid-State NMR Data and Rosetta Modeling

Nikolaos Sgourakis5; Antoine Loquet1, 2, 3; Adam Lange4; David Baker5; 1Max Planck Institute for Biophysical Chemistry,

Göttingen, Germany; 2Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 3Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 4Max Planck Institute, Goettingen, Germany; 5University of Washington,

Seattle, WA Filamentous protein assemblies play an essential role in many bacterial and cellular processes, notably in bacterial virulence. Here, we describe a complete atomic model of the Salmonella typhimurium type three secretion system needle with clearly defined supramolecular interfaces, obtained using a combination of solid-state NMR, sparse 13C labeling protocols, and Rosetta modeling. We find that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns similar to the flagellar filament of Salmonella typhimurium. The final models are validated using biochemical assays that confirm the relative orientation of the subunits. We propose a general framework for the NMR-based modeling of similar higher-order supramolecular assemblies using solid-state or solution NMR data.

ThOD 5:20-5:35

Improved Knowledge-Based Torsion-Angle Potentials Yield Higher-Quality NMR Structures of Proteins Guillermo A. Bermejo; G. Marius Clore; Charles D.

Schwieters; National Institutes of Health, Bethesda, MD Torsion-angle probability densities extracted from a database of X-ray protein models can be converted into so-called knowledge-based potential energy terms that improve structural validation criteria and accuracy of calculated protein NMR structures. However, inspection of current energy surfaces reveals roughness and other features unsupported by angular populations in a modern database. Here, a complete reformulation of the potentials addresses such deficiencies. Smooth, continuous densities, generated from a high-quality database via adaptive kernel density estimation, were converted into energy terms, robustly approximated by cubic interpolation during structure calculations. When tested on nine proteins, the resulting energy surfaces, which are both smoother and sharper, further improve conformational validation criteria, atomic interactions (clashes, packing), and agreement with cross-validated residual dipolar couplings.

ThOD 5:35-5:50

High Pressure MAS NMR Flaviu Turcu; David Hoyt; Jesse Sears; Kevin Rosso; John Loring; Jian Zhi Hu; Pacific Northwest National Laboratory,

Richland, WA Despite its wide spread application, the technique of Magic Angle Spinning (MAS) at pressure exceeding 70 bars has not been possible until recently using a 9.5 mm Zirconium MAS rotor sleeve. Here, we report a new and improved modular design that can be applied for different rotor diameter sizes, compatible with commercial available probes (6 to 9.5 mm standard MAS probes). Using a 7.5 mm alumina-reinforced Zirconium ceramic MAS rotor sleeve, a high pressure MAS rotor capable of 300 bar at a sample spinning rate of 3.5 kHz, or 150 bar at 8 kHz spinning rate, was successfully developed.

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4:00 – 5:50 pm, THURSDAY AFTERNOON ENC FOCUS: NMR IN LATIN AND SOUTH AMERICA

A. J. Shaka, presiding Trianaon

ThOE 4:00-4:25 Dynamically Induced Decoherence Observed through a

Loschmidt Echo in NMR Patricia Rebeca Levstein1, 2; Claudia Marina Sánchez1; Ana Karina Chattah1, 2; Rodolfo Hector Acosta1, 2; Horacio Miguel Pastawski1, 2; 1FAMAF, Universidad Nacional de Córdoba, Córdoba, Argentina; 2IFEG-CONICET, Córdoba, Argentina

I will show a noticeable correlation between the rate at which spin clusters grow in the nematic 5CB, subject to a dipolar evolution, and the decoherence rate. A typical MQC-NMR experiment, governed by a rotated dipolar Hamiltonian, allows for spin counting and the time reversal that produces a Loschmidt Echo (LE). The results indicate that the rate of decoherence can slow-down when changes in the system decrease, even if there are already a significant number of correlated spins. Reciprocally, decoherence can be very fast even with a low number of correlated spins, as long as the system is rapidly changing. Thus, dynamics seems to induce a higher sensitivity to perturbations precluding a perfect LE.

ThOE 4:25-4:50

Multi-quantum Echoes in GdAl2 Zero-field NMR Joao Teles; Jose R. Tozoni; Rodrigo Oliveira-Silva; Ruben

Auccaise; Christian Rivera-Ascona; Edson L. G. Vidoto; Tito J. Bonagamba; IFSC - USP, Sao Carlos, Brazil

We performed zero-field NMR experiments for the intermetallic compound GdAl2 at 4.2 K. Using two RF pulses, we obtained multi-quantum echoes for the 27Al nuclei, which were used for constructing the spectra. The spectra obtained from the FID's observed after the second pulse and the even echoes presented higher resolution than the odd ones. To explain such behavior, we propose a model in which there are two regions inside the sample with different inhomogeneous broadenings. To better understand the origin of the multi-quantum echoes, observe individually the echoes and respective quadrupole oscillations, and simplify the spectral analysis, we implemented coherence selection of the multi-quantum states by phase cycling the RF pulses. Similar data were obtained for 155Gd and 157Gd nuclei.

ThOE 4:50-5:05

How to Measure the Performance of Automated Structure Verification Systems using Negative Control Structures Gonzalo Hernández; Vis Magnetica, Montevideo, Uruguay

Automated Structure Verification (ASV) systems are design to check the consistency between a proposed structure (PS) and the NMR data. Lacking in current ASV implementations is the generation of negative control structures (NCS) from which to challenge the results obtained with the PS. A critical parameter for the proper use of NCS in ASV is a measure of the similarity between NCS and PS in terms of their expected data. It is possible to calculate this similarity through the MolSimNMR method. In this communication I will approach the problem of comparing the performance of different ASV systems and show that it is possible to use the MolSimNMR similarity coefficient to rank, or grade, the performance of different ASV implementations.

ThOE 5:05-5:20 Synthesis and Characterization of 6-bromo-4-(4-chloro-phenyl)-8-methoxy-quinoline by NMR Spectroscopy and

X-Ray Diffraction Ligia Llovera; USB, Caracas, Venezuela

We realize the synthesis and characterization of 6-bromo-4-(4-chloro-phenyl)-8-methoxy-quinoline (2) by NMR spectroscopy and X-Ray Diffraction. The compound crystallizes in the form of light yellow block in a monoclinic cell with dimensions a= 24.666 (11), b= 8.958 (3), c= 17.537 (8) Å, space group C2/c and one molecule in the unit cell.

ThOE 5:20-5:35

Role of Excited States Characterized by NMR in the Catalytic Cycle of Yeast Thioredoxin 1-Thermodynamic

Characterization of Water Permeation Luciana Elena Machado; Federal University of Rio de Janeiro,

Rio De Janeiro, Brazil The aim of this work is to characterize the intermediate excited states of yeast Trx1. We identified a water permeable intermediate state important for function. We measured the dynamics at different temperatures and pHs. Residue Asp24, which is bound to a tightly bound water molecule, modulates the slow dynamics of Trx1. pH modulates conformational exchange. We correlated the pH modulation with the protonation of Asp24. Higher pHs increased conformational exchange, because of the higher desolvation energy of the dissociated Asp24. Water exchange in the vicinities of Asp24 modulates slow conformational dynamics of Trx1. pH and temperature effects indicate a correlation between the protonation, solvation of Asp24 and conformational dynamics. Keywords: Thioredoxin, dynamics, NMR, pH, temperature. Support: CAPES, CNPq, FAPERJ, INCT-INBEB.

ThOE 5:35-5:50

Analysis of the Folding Functions and a Dynamic Approach to the Problem of Optimizing Spectral Widths

in 2D NMR Experiments José Félix Gómez-Reyes; Armando Ariza-Castolo;

CINVESTAV, México D.F., México The modulo function that describes the folding of an NMR signal was reduced to a form of a floor function. An analysis of this function and its graph was realized. The overlap of two signals was also investigated by analyzing the points of intersection of two floor functions. Different expressions that describe the graphs were derived. Based on the properties of the graphs and on the derived expressions was designed a new algorithm to ressolve the problem of optimizing spectral widths in the 13C dimension of heteronuclear 2D experiments. A Folded HSQC spectrum of cholesterol acquired with the calculated spectral width by this method could be unambiguously assigned.

ABSTRACTS OF TALKS

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8:30 – 10:10 am, FRIDAY MORNING FRONTIERS

Tatyana Polenova, presiding Versailles

FOA 8:30-8:55 NMR with a Single Proton

Stefan Ulmer; Holger Kracke; RIKEN Advanced Science Institute, Saitama , Japan

Spin-flips with a single proton were observed for the first time. The spin transitions are detected via the continuous Stern-Gerlach effect, which has been applied already to compare the magnetic moments of the electron and the positron. These experiments involved magnetic moments on the level of the Bohr-magneton. while the proton's magnetic moment is about 660 times smaller and spin-flips are much harder to detect. The first observation of spin flips with one proton is a major step towards a high-precision measurement of the particle’s magnetic moment at the level of 10-9. Since the techniques developed for the proton can be directly transferred to the antiproton, this is a crucial milestone towards a million-fold improved test of matter-antimatter-symmetry with baryons.

FOA 8:55-9:20

Cellular Solid-State NMR Spectroscopy Marie Renault; Martine Bos; Eline Koers; Ria Tommassen-van

Boxtel; Mohammed Kaplan; Jan Tommassen; Marc Baldus; Utrecht University, Utrecht, Netherlands

Decrypting the structure and organization of complex molecules in their cellular context is of prime importance for understanding fundamental physiological processes. Nuclear Magnetic Resonance is a well-established imaging method that can visualize cellular entities at the μm scale and can be used to obtain 3D atomic structures under in-vitro conditions. Here, we introduce a solid-state NMR (ssNMR) approach that provides atomic level insights into cell-associated molecular components. By combining dedicated protein production and labeling schemes with tailored ssNMR pulse methods, we obtained structural information of a recombinant integral membrane protein and the major endogenous molecular components in a bacterial environment. Our approach permits studying entire cellular compartments as well as cell-associated proteins at the same time and at atomic resolution.

FOA 9:20-9:35

Molecular Spins: a New Frontier of Chemical Physics and Magnetic Resonance?

Stanislav Sykora; Extra Byte, Castano Primo, Italy This presentation conjectures – and defends - the idea of the existence of persistent electron current loops in diamagnetic molecules whose structures make it possible, from a purely geometric point of view, to associate a fixed axial vector with them (example: all molecules of the type O=C(XY), where X,Y are distinct atoms or groups. If the insight is correct then such molecules should possess an intrinsic spin and a permanent magnetic moment, thus enabling magnetic resonance phenomena similar to those associated with nuclides and giving birth to Molecular Magnetic Resonance (MMR). There is also a good chance that the overlooked persistent electron current loops represent a factor which presently hinders a forward leap of quantum chemistry methods such as DFT.

FOA 9:35-9:50 Optically Detected NMR Relaxometry in Low Magnetic

Field Paul Ganssle1, 2; Hyun Doug Shin1, 2; Scott Seltzer1, 2; Vikram S. Bajaj1, 2; Dmitry Budker2, 3; Svenja Knappe4; John Kitching4;

Alex Pines1, 2; 1UC Berkeley, Dept. of Chemistry, Berkeley, CA; 2Lawrence Berkeley National Labs, Berkeley, CA; 3UC

Berkeley, Dept. of Physics, Berkeley, CA; 4Time and Frequency Division, NIST, Boulder, CO

In this work, we demonstrate the use of an atomic vapor-cell magnetometer to measure the relaxation and diffusion properties of protons in water and hydrocarbons, and look at the chemical sensitivity of the technique in both pure and mixed samples, with potential industrial applications including oil well logging. Samples are pre-polarized at 1T and shuttled to a zero-field detection region, where T-1, T2 and diffusion coefficients at 0.5 G are detected in an indirect dimension by field cycling the samples. Data already collected clearly demonstrate the chemical distinguishability of water and several different hydrocarbons, and indicate strong potential to distinguish the components of mixtures.

FOA 9:50-10:05

A Spinning Permanent Magnet for Magic Angle Field Turning

Cedric Hugon2; Dimitrios Sakellariou1; 1CEA Saclay, Gif-Sur-Yvette, France; 2École Normale Supérieure, 24 rue Lohmond,

Paris, France Magic Angle field spinning has been proposed very early by R. Andrew [1]. This experiment could offer unique information in cases where the sample spinning at the magic angle is not possible or wanted. In the past we have a developed a methodology to build homogeneous permanent magnets for NMR and MRI [2]. We have built the first high-resolution pure permanent magnet [3], generating a strong magnetic field along the magic angle with respect to its axis of rotation. We will present experiments where the magnet is static and slowly spinning around a static sample. Novel ideas about imaging in these conditions as well as shimming in the presence of spinning fields or samples will also be presented.

ABSTRACTS OF TALKS

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10:45 am – 12:20 pm, FRIDAY MORNING LARGE SYSTEMS

Chad Rienstra, presiding Versailles

FOB 10:45-11:10 Solution NMR Studies of Membrane Transporters James Chou; Harvard Medical School, Boston, MA

Membrane transporters usually undergo large conformational changes during the transport of substrates. For many of the transporters, obtaining detailed structures and dynamics information of multiple functional states has been difficult. We have been exploring the use of solution NMR to study passive transporters and have developed a system for structural characterization of mitochondrial uncoupling protein 2, a member of the carrier family that translocates protons across the inner membrane. The method combines RDC-based molecular fragment replacement and semi-quantitative distance restraints from paramagnetic relaxation enhancement measurements. We believe this biophysical approach can potentially play an important role in studying transporter mechanism, and have already applied it to investigate the mechanism of nucleotide transport of other mitochondrial carriers.

FOB 11:10-11:35 Parameterization of Solvent-Protein Interaction and Its

Use on NMR Protein Structure Determination Yu Wang1; Charles D. Schwieters2; Nico Tjandra1; 1NHLBI, National Institutes of Health, Bethesda, MD; 2CIT, National

Institutes of Health, Bethesda, MD Due to the lack of complete structural information, obtaining a correct fold of a protein in the initial stages of NMR structure determination can be challenging. To solve this problem we introduce an empirical energy into Xplor-NIH to incorporate restraints based on measurements of interaction between protein and solvent. We demonstrate this approach using a solvent paramagnetic relaxation data set on a homodimer protein Qua1 and water to protein magnetization transfer data on the protein Bax. The calculated solvent accessibility values using the new empirical function are well correlated with the experimental data. We show that structure calculation using the new empirical energy with a limited number of experimental restraints, improves both the precision and accuracy of the resulting structures.

FOB 11:35-11:50

Experiments Optimized for Rotationally Aligned Solid-State NMR of Membrane Proteins in Proteoliposomes

Bibhuti Das; Stanley J. Opella; University of California, San Diego, La Jolla, CA

Rotational Alignment (RA) solid-state NMR provides basis for a general method for determining the structures of membrane proteins in phospholipid bilayers under physiological condition1. The method merges elements of oriented sample (OS) solid-state NMR and magic angle spinning (MAS) solid-state NMR to measure orientation restraints relative to the bilayer normal2. Measurement of 1H-15N and 1H-13C dipolar couplings from unoriented samples using MAS solid-state experiments provides relatively high resolution for the identification of residue types and structural characterization of membrane proteins. These experiments can be performed in combination with conventional MAS solid-state NMR experiments to fully resolve and assign spectra of membrane proteins with between one and seven transmembrane helices.

FOB 11:50-12:05 Magic Angle Spinning Dynamic Nuclear Polarization NMR

at 700 MHz/460 GHz Vladimir K. Michaelis1; Eugenio Daviso1, 2; Evgeny

Markhasin1; Alexander B. Barnes1; Emilio A. Nanni1; Sudheer K. Jawla1; Ajay Thakkar1; Ronald DeRocher1; Judith

Herzfeld2; Richard J. Temkin1; Robert G. Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA;

2Brandeis University, Waltham, MA NMR is a powerful spectroscopic technique, which can be used to determine protein structure and dynamics. Unfortunately the low sensitivity often limits multi-dimensional NMR experiments where further structural information can be gained. To gain further structural information by boosting sensitivity and spectral resolution, the development of an high field 700 MHz/460 GHz DNP NMR spectrometer is presented with recent results. A series of small molecules and biological solids were studied using the bi-radical TOTAPOL as a polarizing agent. The current configuration operates above 15W of microwave power and performs MAS based experiments at 80K providing a 40-fold enhancement on U-13C-Urea using CPMAS. Two-dimensional 13C-13C DARR experiments on U-13C-Proline and large biological systems will also be discussed illustrating enhancements upto 30x.

FOB 12:05-12:20

Paramagnetic mapping of the 116 kDa Ca2+ATPase/phospholamban membrane protein complex

in lipid bilayers by solid state NMR spectroscopy Martin Gustavsson1; Raffaello Verardi1; Nathaniel J

Traaseth2; Gianluigi Veglia1; 1University of Minnesota, Minneapolis, MN; 2New York University, New York, NY

Ca2+-ATPase (SERCA) and phospholamban (PLN) form a 116 kDa membrane protein complex that regulates cardiac muscle relaxation. Here, we used a combination of solid state and solution NMR (hybrid method) to characterize the structure of the SERCA/PLN complex. We utilized magic angle spinning (MAS) experiments in native-like lipid vesicles to confirm that SERCA-bound PLN populates multiple conformational states and determined the secondary structure of these states. PRE experiments showed that SERCA selectively interacts with and unfolded conformation of PLN and provided multiple protein-protein contacts between the proteins. Chemical shifts, PRE restraints, chemical shift perturbations and orientational restraints from separated local field (SLF) experiments were utilized to calculate structures of the different conformational states of PLN in complex with SERCA.

POSTERS All posters should be set up 8:00 to 9:00 am on Monday and removed at 3:45 pm on Thursday. Be sure to use the poster space number printed

here. Authors of odd-numbered posters present on Monday and Wednesday. Even numbered posters present on Tuesday and Thursday.

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ATRIUM Page Biomolecular NMR, 001 - 060 ........................................ 44 Biomolecules, 061 - 069 ................................................ 54 Calculations & Simulation, 070 - 084 ............................. 55 Detection, 085 – 087 ..................................................... 58 Diffusion & Flow, 088 – 099 ........................................... 58 Dynamics, 100 - 113 ...................................................... 60 Education/Facilities, 114 – 115 ...................................... 62 Exotica & Beyond, 116 – 126 ........................................ 63 Hyperpolarization & New Detection Methods,

127 – 163 ............................................................... 65 in vivo NMR Spectroscopy, 164 – 170 ........................... 71 Instrumentation, 171 – 187 ............................................ 72 Instrumentation/ Large Systems, 188 – 189 .................. 75 Liquids Methods: Biomolecules, 190 - 203 .................... 75 Liquids Methods: Small Organic Molecules,

204 – 225 ............................................................... 77 Liquids: New Applications, 226 - 233 ............................. 81 Materials, 234 – 240 ...................................................... 83 Metabolism, Mixture Analysis & Statistics, 241 - 254 .... 84 Motion & Dynamics, 255 – 257 ...................................... 86 MRI, 258 – 261 .............................................................. 87 NMR & Crystallography, 262 - 268 ................................ 87 NMR Imaging: Advances, 269 – 270 ............................. 88 Resolution & Sensitivity, 271 - 272 ................................ 89 Screening, 273 – 274 .................................................... 89 Small Molecules & Drug Discovery, 275 - 298............... 89 Software & Hardware, 299 – 306 ................................... 93

CHOPIN BALLROOM Solids: Bio-Applications, 307 - 337 ................................ 95 Solids: Inorganics & Materials, 338 – 357 ................... 100 Solids: Methods, 358 – 381 ......................................... 103 Solids: Small Molecules, 382 – 389 ............................. 107 Posters of Contributed Talks, 390 - 412 ...................... 108

BIOMOLECULAR NMR, 001 - 060

Poster 001

Glycosaminoglycan Characterization through Sulfamate Analysis by 1H and 15N NMR Spectroscopy

Derek Langeslay; University of California, Riverside, CA Sulfamate groups (NHSO3-) are important structural elements of the glycosaminoglycans (GAGs) heparin and heparan sulfate (HS). Recently, our group reported solution conditions that permit detection of the resonances of sulfamate NH groups in oligosaccharides and in the low molecular weight heparin Enoxaparin. This discovery permits, for the first time, the opportunity to study the exchange properties of the sulfamate protons through line shape analysis. The effects of pH and temperature on the solvent exchange of the sulfamate protons will be presented for a series of heparin-related oligosaccharides. The results obtained for the pentasaccharide drug Arixtra (Fondaparinux) indicate the presence of a persistent hydrogen bond between the sulfamate group NH and the adjacent 3-O sulfo group of the central glucosamine residue.

Poster 002

NMR Study of the Effect of Dilution on Isotropic Bicelles and Development of DPC-based Bicelles

Maïwenn Beaugrand1; Alexandre A. Arnold1; Philip T.F. Williamson2; Isabelle Marcotte1; 1Université du Québec à

Montréal, Montréal, Canada; 2University of Southampton, Southampton, UK

Bicelles are model membranes used in the study of membrane-protein (MP) interactions and structure by NMR. However, experimental constraints may require their use at high dilutions at which their morphology is unclear. Following the 31P NMR chemical shift of DHPC at several DMPC/DHPC (q) ratios, a “critical bicellar concentration” was calculated and shown to decrease with increasing q ratios. Bicelles morphology is similar to the native environment of membrane proteins. To improve the solubilization of such proteins in bicelles, we have developed dodecylphosphocholine-based bicelles. These are promising model membranes that should be amenable to both solution- and solid-state NMR, thus enabling structure determination and lipid interaction studies with a single membrane mimicking system.

Poster 003

Accurate Reduced Spectral Density Mapping for Analysis of 13-C Relaxation Rates

Pavel Kaderavek; Vojtech Zapletal; Radovan Fiala; Vladimir Sklenar; Lukas Zidek; Masaryk Univ, Brno, Czech Republic

NMR can provide both the structural and dynamical information about the investigated biomolecules. The analysis of ps-ns motions is usually based on experimental relaxation rates of I-S spin pairs. A spectral density mapping is used as a robust method utilizing linear combinations of measured data. Reduced spectral density mapping is usually used for the analysis of 15N-1H spin pairs relaxation but this approach is not suitable for analysis 13C-1H relaxation rates. Therefore we developed an alternative approach based on combining data measured at various magnetic fields. If the ratio of fields strength is equal to 3:4:5, exact spectral density values are obtained. The proposed approach has been successfully applied to an RNA hairpin molecule including the UUCG loop.

Poster 004

Solution-state NMR Structures and Molecular Dynamics Simulations of The Eye Lens Protein gammaS-crystallin

William Brubaker; Alfredo Freites; Carolyn Kingsley; Douglas Tobias; Rachel W. Martin; UC Irvine, Irvine, CA

Here we present solution structures of the wild-type gammaS-crystallin and the G18V variant, which has been cilnically linked to an autosomal dominant child-onset cataract in humans. A detailed comparison of the NMR structures of wild-type and G18V highlights the structural changes involved in cataract formation in humans and will allow more accurate modeling of protein stability and solubility in cataract formation and other diseases involving protein aggregation. We outline key structural changes explaining the observed differences in thermodynamic stability and solubility in variants of gammaS-crystallin using both solution-state NMR data and information from molecular dynamics simulations. These structural shifts highlight important structural motifs that are responsible for stabilizing the double Greek key fold common to all beta/gamma-crystallins.

Poster 005

NMR Study of the Structure, Function and Role of the hERG Channel Selectivity Filter Involved in the Long QT

Syndrome Andrée Gravel; Alexandre A Arnold; Isabelle Marcotte; Université du Québec à Montréal, Montréal, Canada



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The acquired long QT syndrome (ALQTS) is a drug side effect responsible for heart arrhythmia or failure. This cardiac disorder is due to the blockage of the heart’s human ether-a-go-go-related-gene (hERG) potassium channel. The hERG channel is a unique member of the voltage-gated K+ channel family because of its particular selectivity filter (SF) sequence. We have studied the structure and interaction of the hERG’s SF with model membranes and cardiotoxic drugs by solution and solid-state nuclear magnetic resonance (NMR). Our results demonstrate the unstructured nature of the SF in an aqueous environment, as well as the possible involvement of the SF and membrane in the ALQTS.

Poster 006

Structural and Dynamics Studies of CAP-Gly Domain of Mammalian Dynactin by Magic Angle Spinning NMR

Spectroscopy Si Yan1; Guangjin Hou1; Charles Schwieters2; John Williams3;

Tatyana Polenova1; 1University of Delaware, Newark, DE; 2National Institutes of Health, Bethesda, MD; 3Beckman

Research Institute of City of Hope, Duarte, CA We present the 3D structure of a microtubule binding protein, CAP-Gly domain of mammalian dynactin, determined with high accuracy by using an R2-symmetry driven spin diffusion (RDSD) sequence for MAS NMR spectroscopy. Our results indicate two conformations present in the vicinity of residue A45, and unique flexibility in loop regions, especially in the GKNDG motif. To probe the conformational dynamics of CAP-Gly, we have conducted site-specific measurements of 15N-1H dipolar and 15N CSA lineshapes at different temperatures, and the 15N spin-lattice relaxation rates in the rotating frame under fast MAS conditions. Large variability was observed in these NMR parameters, indicating significant mobility of the CAP-Gly domain on the micro- and nanosecond timescales, particularly in the loop regions.

Poster 007 Structure of the Ubiquitin-associated (UBA) Domain of

p62 and Its Interaction with Ubiquitin Hidehito Tochio; Kyoto University, Kyoto, Japan

p62/SQSTM1/A170 is a multimodular protein found in ubiquitin-positive inclusions associated with neurodegenerative diseases. p62 has been proposed to mediate the interaction between ubiquitinated proteins and autophagosomes, leading the ubiquitinated proteins to degradation via the autophagy-lysosomal pathway. In this study, the crystal structure of the UBA domain of mouse p62 and the solution structure of its ubiquitin-bound form are presented. The revealed dimeric structure of the p62 UBA domain in crystals is substantially different from those of other known UBA dimers. The structures indicated that dimerization and ubiquitin binding of the p62 UBA domain are mutually exclusive, suggesting an autoinhibitory mechanism in the p62 UBA domain, which may play an important role in the function of p62.

Poster 008

Interrogation of Membrane Binding of Toxin C1 Domains to Anionic Phospholipids

Michael Brothers1; Brett Geissler2; Brenda Wilson1; Karla Satchell2; Chad Rienstra1; 1University of Illinois, Urbana, IL;

2Northwestern University, Chicago, IL

Understanding how bacterial AB toxins interact with membranes is important to the generation of therapeutics and anti-virulence drugs. Of interest is a class of 38 homologous four-helical bundle localization domains that target anionic phospholipids and studying membrane binding as a function of the residue in a putative hydrophobic insertion motif (Phe v. Ile v. Thr). We are using a joint solution NMR/SSNMR approach to interrogate chemical shifts in solution, bound to micelles, and bound to liposomes in order to understand membrane interactions. We have complete assignments of the solution state for C1PMT and resolved 3D spectra for VVDUF5. We acquired 2D HC spin-diffusion spectra and determined the helical bundle is surface-associated and look now towards membrane insertion.

Poster 009

SSNMR Study of the Structure and Function of Anionic Phospholipid Membranes in Blood Coagulation

Mary Clay; John Boettcher; Rebecca Davis-Harrison; Taras Pogorelov; Zenmei Ohkubo; James Morrissey; Emad

Tajkhorshid; Chad Rienstra; University of Illinois at Urbana-Champaign, Urbana, IL

Exposure of phosphatidylserine (PS) to plasma concentrations of calcium triggers the formation of PS-rich nanodomains, which are proposed high affinity binding sites for coagulation factors. There is no clear description of these PS-nanodomains or explanation for how they regulate coagulation reactions. We used magic-angle spinning solid-state NMR (MAS SSNMR) and 13C, 15N-labeled PS headgroups to develop an atomic resolution description of the structure and dynamics of PS-rich nanodomains and their interaction with GLA domains. SSNMR spectra of POPC/POPS* bilayers demonstrate that Ca2+ promotes two configurations of the PS headgroup. We also identified a third configuration of the PS headgroup induced upon insertion of the GLA domain, with a relative intensity that was consistent with one-PS specific binding interaction per GLA domain.

Poster 010

Assignments and Dynamics of the 46 kDa DNA Polymerase β-DNA Complex

Eugene F DeRose1; Thomas Kirby2; William Beard2; Samuel Wilson2; Robert London2; 1NIEHS Contractor, Research Triangle Park, NC; 2NIEHS, Research Triangle Park, NC

We have studied the dynamics of a 46 kDa DNA polymerase β-DNA complex using 13C-methionine labeling. Interesting changes indicative of intermediate exchange dynamics of the protein were observed upon formation of abortive protein-DNA-nucleotide ternary complexes. We have assigned the methyl groups of isoleucine, leucine, and valine sidechains in the protein complex and plan to carry out additional methyl relaxation dispersion experiments to more fully characterize the dynamics of these ternary complexes.

Poster 011 Tackling Sizeable RNA Problems by NMR using Site

Alternate Isotopic Labeling Strategies T. Kwaku Dayie; University of Maryland/Chemistry

Department, College Park, MD RNAs are central to many cellular processes, and this functional dexterity depends on RNAs ability to remodel their 3D architectures to bind various ligands using either induced fit, or conformational capture, or both. Thus NMR methods can be applied to probe how dynamics modulates function.



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However, accurately determining these dynamical parameters by solution NMR can be problematic using existing labeling methodologies. To circumvent these problems, we have developed an effective selective labeling technology that allows more accurate measurements of relaxation parameters. We will discuss applications to various RNA model systems. Overall the tools we have developed should be broadly applicable to many exciting and interesting emerging RNA biological problems.

Poster 012

Transmembrane Heterodimer Packing using Topology and Sparse Distance Restrains

Frantz L. Jean-Francois; NHMFL, Tallahassee, FL Solid state NMR and EPR are powerful techniques to study protein structure and interaction within the membrane hydrophobic core. Recent results highlight the role of hydrophobic peptides that form a novel class of active molecules acting on membrane proteins through hydrophobic interactions. To further understand this new mechanism at a molecular level, the interaction between two potentially interacting peptides is studied. This system is made of the potential drug, MgtR, one of these newly discovered hydrophobic peptides, and its potential target (MgtC) involved in the Tuberculosis latent state. These two peptides were chemically synthesized and reconstituted into DMPC bilayers aligned on glass plates. The interaction is examined by using solid state NMR PISEMA spectra of aligned samples and CW EPR.

Poster 013

Accurate Dynamics Measurements of A-site RNA using 13C and 15N Selectively Labeled Nucleotides

Regan Leblanc; University of Maryland, College Park, MD Dynamics plays an important role in the function of many regulatory and catalytic RNAs. By utilizing 13C and 15N site specifically labeled nucleotides, grown in E. coli from labeled precursors, we can measure the motions on the NMR timescale without interference from large scalar and residual couplings known to occur in uniformly labeled samples. We used our specifically labeled nucleotides to compare dynamics measurements in A-site RNA, a model molecular switch system, with measurements obtained using uniformly labeled nucleotides.

Poster 014

Towards a Kinetic and Thermodynamic Characterization of Rate-Limiting Motions in RNase A

Gennady Khirich; J. Patrick Loria; Yale University, New Haven, CT

Dynamics on the us-ms timescale, much like structure, are critical in maintaining the catalytic integrity of an enzyme. In Ribonuclease A (RNase A), the rate-limiting step in the catalysis of the cleavage of single-stranded RNA is a conformational change. In the absence of substrate the enzyme exists in an equilibrium mixture, sampling the high energy bound form ~5% of the time. This process is thought to be mediated by the protonation state of a distal histidine (H48) situated within a cluster of hydrogen bonds. In the current study, the pH and temperature dependence of ms motions, characterized by CPMG relaxation dispersion experiments are used to characterize the

kinetics and thermodynamics which govern these rate-limiting conformational motions in RNase A.

Poster 015

Adapting Standard Protein NMR Sequences for High-field Applications

Evgeny Tishchenko; Agilent Technologies, Santa Clara, CA One of the problems with protein NMR that involves 13C nuclei at high fields (800+ MHz) is that one is no longer able to efficiently refocus the full 13C range with hard (rectangular 13C) 180 pulses. In high-field applications, the performance of many well-established experiments utilizing those hard 180pulses can become substandard. Here we present an example of how the extensive use of Broadband Inversion Pulses (BIP) in the widely used NOESY-13C-HSQC experiment allows one to record spectra covering the entire methyl-to-aromatics 13C region with uncompromised sensitivity and superior water suppression. Pulse sequence implementation details are discussed; the experiment is now available in standard BioPack library from Agilent.

Poster 016 Solid-state NMR Studies of caveolin-1 Protein and Peptides Reconstituted in Cholesterol-containing

Membranes Yanli Zhang; Sorin Luca; University of Nebraska Medical

Center, Omaha, NE Caveolae are omega-shaped invaginations of the cellular membrane that are involved in cellular signaling and transport. Caveolae structural integrity is maintained by caveolins which act as membrane scaffolding proteins. We report here the successful preparation of pure human caveolin-1 (hCav1) and its membrane domain (hCav1*) in milligram amounts. Subsequent high-yield reconstitution of hCav1/hCav1* in cholesterol-containing model membranes is also reported. The resulting proteoliposomes are homogeneous as shown by atomic force microscopy, dynamic light scattering and circular dichroism. Furthermore hCav1 is correctly folded as demonstrated by its interaction with caveolin binding domain from HIV-1 glycoprotein gp41. Preliminary solid-state NMR experiments indicate protein structural homogeneity at the molecular level.

Poster 017

Evaluation of NMR Relaxation Data for Comparison of Mutation Effects in HIV-1 Protease

Wazo Z. Myint; Rieko Ishima; University of Pittsburgh, Pittsburgh, PA

The dynamics of HIV-1 protease (PR) have been previously studied to optimize design of inhibitors since protease activity is essential for the lifecycle of the HIV-1 virus. NMR and other spectroscopic methods have shown that the flap region, known to be important for catalytic activity, undergoes significant internal motion. In this study, 15N relaxation experiments were performed to identify differences in backbone dynamics between the wild type PR and one of the multidrug-resistant mutants that contain mutations in the flap region. For comparison of flap dynamics due to mutation effects, we reexamined the methods used in the processing and error analysis of 15N relaxation parameters, the model selection criteria in model-free analysis, and the evaluation of R2 relaxation dispersion data.



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Poster 018 Towards Structural Characterization of Synthetic Mouse

Prion Strains by MAS SSNMR Aleksandra Kijac1, 2; Jan Stöhr1; Lindsay J. Sperling2; Julia Becker1; Holger Wille1; Alex Pines3; Stanley B. Prusiner1;

Vikram S. Bajaj3; David E. Wemmer 3; 1University of California San Francisco, San Francisco, CA; 2Lawrence Berkeley

National Laboratory, Berkeley, CA; 3University of California, Berkeley, Berkeley, CA

Prion diseases are fatal neurodegenerative disorders associated with the misfolding, oligomerization, and deposition of insoluble protein aggregates in the brain. The transmissibility of prion diseases to animal and cellular models makes them an experimentally tractable paradigm that allows for investigation of the relationship between structural changes that lead to protein misfolding and oligomerization and disease pathogenesis. Synthetic prion strains were created by the in-vitro conversion of recombinant prion protein into infectious conformers. We describe use of a number of biochemical methods to characterize synthetic prion strains and magic-angle spinning (MAS) SSNMR to obtain direct structural information, which can then be correlated to the distinct disease phenotypes observed upon inoculation of transgenic mice models with the same synthetic prion strains.

Poster 019

Human Insulin and Its Analogues, Aggregation and Dynamics Studies by NMR

Wojciech Bocian1; Elzbieta Bednarek1; Jerzy Sitkowski1; Piotr Borowicz2; Dariusz Kurzynoga2; Diana Mikiewicz-Syguła2; Bożena Tejchman-Małecka2; Monika Pawłowska2; Lech

Kozerski1; 1National Medicines Institute, Warsaw, Poland; 2Institute of Biotechnology and Antibiotics, Warsaw, Poland

Here we characterize insulins with an additional amino acid at the C-terminus of the A chain, A22G, which interacts with the β-turn environment of the B chain resulting in high flexibility of the B chain C-terminus. A tertiary structures of recombinant insulins are characterized by 1H, 13C NMR at natural isotopes abundance using NOESY, TOCSY, 1H/13C-GHSQC, and 1H/13C-GHSQC-TOCSY spectra. The high mobility of the B chain C-terminus in modified insulins are supported by the analysis of RCI (Random Coil Increment). Detailed analysis using PFGSE NMR, dilution and titration experiments proves the existence of complex insulin aggregate states in water over a range of μM to mM with strong dependence on pH.

Poster 020

Chemistry and DNA-complexes of Topoisomerase I Inhibitors

Elzbieta Bednarek1; Wojciech Bocian1; Jerzy Sitkowski1; Beata Naumczuk2; Lech Kozerski1, 2; 1National Medicines Institute, Warsaw, Poland; 2Institute of Organic Chemistry,

PAS, Warsaw, Poland Topotecan (TPT) acts by binding to the covalent complex formed between nicked DNA and topoisomerase I and inserts itself into the single-strand nick, inhibiting the relegation of the nick and acting as a poison. NMR spectroscopy and molecular modeling were used to investigate TPT structure in water and structure of nicked DNA binding to Topotecan or product of quaternization of nitrogen in Topotecan. We demonstrate that only nicked DNA is target for TPT and it intercalates into the nick, essentially lengthening the DNA.

TPT is stacking against a GC base pair. The aim of this research is to provide a greater understanding of the binding of topoisomerase I inhibitors to nicked DNA to assist in designing improved drugs

Poster 021

Structure Determination of a 170 Amino Acid Target Using RASREC-Rosetta and Limited Experimental

Constraints Timsi Rao; Geoffrey S Armstrong; Deborah Wuttke; University

of Colorado, Boulder, CO We present the NMR structure determination of a challenging target protein 170 amino acids in length, which required perdeuteration in order to complete the NMR characterization. This coupled with stability issues and relaxation properties precluded traditional structure determination. Aided by the Janus supercomputer at the University of Colorado, we attempted structure determination using RASREC-Rosetta. The NMR experimental data included backbone chemical shifts as well as amide RDCs, amide-amide NOEs, and ILV methyl NOEs, resulting in ~400 constraints, with only ~130 long range NOEs. We obtained converged structure ensembles satisfying the experimental constraints. The results were repeatable using different subsets of the experimental constraints, and validated using several available structure analysis methods.

Poster 022

Effect of Metal Binding on the Membrane Association of C1B and C2 Regulatory Domains from Protein Kinase Cα

Krystal A. Morales; Tatyana I. Igumenova; Texas A&M University, College Station, TX

We used NMR to characterize the effect of Pb2+, a potent environmental toxin, on the interactions of C2 domain from PKCα with phosphatidylinositol-4,5-biphosphate (PIP2) and model membranes. We found that Pb2+ and PIP2 enhance each other’s affinity to C2 through the modulation of the protein’s electrostatic properties. This behavior contributes to the toxic effect of Pb2+ resulting from the aberrant modulation of PKCα activity. Based on our data, we propose a mechanism for Pb2+ outcompeting Ca2+ from the membrane-bound C2. Metal-binding studies, extended to the two-domain C1B-C2 PKCα construct, revealed a potential inter-domain rearrangement in the presence of Ca2+. Structural characterization of this construct is currently in progress using a combination of X-ray crystallography and RDC measurements from paramagnetic-induced alignment.

Poster 023

Direct Observation of the pH-Dependent Equilibrium between Open and Closed Conformations of hMGL by

NMR Spectroscopy Sergiy Tyukhtenko; Ioannis Karageorgos; Nikolai Zvonok;

Alexandros Makriyannis; Northeastern University, Boston, MA Monoacylglycerol lipase (MGL) playing a key role as a hydrolyzing enzyme of 2-AG in the endocannabinoid system. Design and development of potent and selective MGL inhibitors require detailed understanding of catalytic mechanism and substrate specificity. We have found that hMGL is in pH-dependent equilibrium between the open and closed forms which does not require presence of detergent or ligand. Interconversion of two forms is reversible and slow on the NMR time scale. Our results demonstrate that this lipase



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provides a unique possibility for the simultaneous NMR detection of both open and closed conformations as well as separate detection of individual forms. Thus the open-closed transition pathways which are mostly unknown for lipases can be directly investigated by NMR in details.

Poster 024

O-antigen and Core Carbohydrate of Vibrio fischeri Lipopolysaccharide: Composition and Analysis of their Role in Euprymna scolopes Light Organ Colonization

Liping Yu; University of Iowa, Iowa City, IA Vibrio fischeri exists in symbiotic relationship with the Hawaiian bobtail squid, Euprymna scolopes, where the squid provides a home for the bacteria and the bacteria in turn provide camouflage that helps protect the squid from nighttime predators. Like other Gram-negative organisms, V. fischeri expresses lipopolysaccharide (LPS) on its cell surface. Here we used NMR, MS, and other methods to study structure and function of LPS of the wild-type and O-antigen ligase mutant V. fischeri. We found that V. fischeri LPS has a single O-antigen repeat composed of unusual sugars of yersiniose and 8-epi-legionaminic acid, and that the mutant has a motility defect, is significantly delayed in colonization, and is unable to compete with the wild-type strain in co-colonization assays.

Poster 025

Structural Characterization of the Human eIF4A/4G Helicase Complex in Translation Initiation

Christian Wasmer; Katherine A. Edmonds; Gerhard Wagner; Harvard Medical School, Boston, MA

The eIF4F protein complex is important for the initiation of protein synthesis and performs regulatory tasks that are especially important in eukaryotes. Its malfunction leads to cancer and other diseases. In this study we investigate the structure of a part of eIF4F, the 66-kDa complex formed by the RNA helicase eIF4A and the HEAT2 domain of eIF4G. We sequentially assigned almost all observable resonances of eIF4A in isolation as well as in the complex with HEAT2. We have structurally characterized this complex using chemical-shift–perturbation mapping and paramagnetic relaxation enhancements induced by a nitroxide spin-label attached to HEAT2. The structural data derived from this and other spin-labeled samples will be used to establish a structural model of the eIF4A–HEAT2 complex.

Poster 026

Molecular Recognition of Paxillin LD Motifs by Pyk2 PAT Domain

Murugendra Vanarotti; St Jude Children's Research Hospital, Memphis, TN

Proline-rich tyrosine kinase 2 (Pyk2) is a multi-domain protein and a member of the focal adhesion kinase (FAK). The C-terminal Pyk2 adhesion targeting (PAT) domain targets Pyk2 to cellular focal adhesion areas, where it interacts with the signaling molecule paxillin. Here we report the complex structures of PAT in complex with leucine-aspartate repeat (LD) motifs (LD2 and LD4) of paxillin. Our structural studies show that two paxillin peptides bind to opposite sides of PAT, α-helices 1/4 (H1/H4) and α-helices 2/3 (H2/H3). The affinity of these LD motifs for PAT is significantly greater for H2/H3 as determined by NMR, ITC and AUC.Thus

suggesting H2/H3 is the relevant paxillin binding site which may be exploited for structure-based drug design efforts.

Poster 027

Precision of NMR-Derived Dissociation Constants for Weakly Interacting Protein-Ligand Pairs

Martin Christen; Rieko Ishima; University of Pittsburgh, Pittsburgh, PA

Protein-ligand interactions are frequently investigated with titration experiments monitored via series of 1H/15N HSQC spectra. While the principle of chemical shift analysis is widely applied, uncertainty remains about how to derive dissociation constant (Kd) values with a meaningful associated error when chemical shift changes are small. Using inhibitor interactions with the RNase domain of HIV-1 reverse transcriptase (RNH) as a model, we systematically investigate the impact of three points of contention on the derivation of a Kd value for a system in fast exchange, namely the effects of 1. the chemical shift uncertainty, 2. the normalization protocol for combining proton and nitrogen shifts and 3. the quantification of chemical shift changes during the titration series.

Poster 028

Modulation of Protein Tyrosine Phosphatase Catalysis by Active Site Loop Motion

Sean Whittier1; Alvan Hengge2; J. Patrick Loria1; 1Yale University, New Haven, CT; 2Utah State University, Logan, UT Protein tyrosine phosphatases (PTPs) are a class of enzymes that catalyze the dephosphorylation of tyrosine residues in intracellular proteins. The active site of PTPs is partially formed by a flexible loop, the WPD-loop, which participates in catalysis. Previous efforts to characterize WPD-loop dynamics have used a variety of techniques, not including NMR, but have failed to find agreement on a timescale for loop motion. It is also not clear what role WPD-loop motion plays in regulating the activity of PTPs. Here we have characterized and compared the dynamics of WPD-loop motion in two separate PTPs using NMR. We find kcat and kex differ by the same magnitude between each enzyme, suggesting WPD-loop motion plays a role in regulating PTP catalysis.

Poster 029

Further Evidence of Hoogsteen Base Pair Transient States in Canonical DNA

Federico Gottardo; University of Michigan, Ann Arbor, MI DNA is known to be a highly dynamic biomolecule involved in a plethora of processes where conformational flexibility is necessary. It’s been recently shown that canonical DNA can undergo chemical exchange from Watson-Crick to Hoogsteen base pair using 13C R1ρ relaxation dispersion. These transient states are low populated (<1%), short-lived (<5ms) and involve a G and T imino hydrogen bond disruption and formation. Here, we directly probe this process by applying for the first time 15N R1rho relaxation dispersion to nucleic acids. Our results are in very good agreement with 13C R1ρ relaxation dispersion, even emulating its chemical exchange pH dependence. Our data gives further support to the presence of transient Hoogsteen base pairs in canonical DNA.



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Poster 030 Structural Characterization of M-TTR Amyloid Fibrils by

Solid-State NMR approaches Flavia Guedes de Andrade1; Ricardo Sant'Anna1; Annete

Diehl2; Carolina Azeredo Braga1; Hartmut Oschkinat2; Debora Foguel1; Mônica Santos De Freitas1; 1UFRJ, Rio De Janeiro,

Brazil; 2Leibniz für Molekulare Pharmakologie, Berlin, Germany

Amyloidosis is a clinical disorder caused by extracellular deposition of proteins that are normally soluble in their native conformation, but suffer conformational modifications resulting in insoluble, abnormal fibrils that impair organ function. Parkinson’s disease (PD) and Alzheimer’s disease (AD) are the two major common neurodegenerative diseases. In this work we are using transthyretin (TTR) fibrils formed from the monomeric construction of TTR protein (MTTR). The solid state NMR data has shown narrow peaks as an indication of well ordered fibrils. However, only few peaks were observed in comparison to the length of the protein that suggest us different degrees of mobility on fibril structure. In this way, a combination of solution and solid-state NMR has been applied in this work.

Poster 031

Fast Hydrogen Exchange Affects 15N Relaxation Measurements in Intrinsically Disordered Proteins

Seho Kim; Kuen-Phon Wu; Jean Baum; Rutgers University, Piscataway, NJ

Unprotected amide protons can undergo fast hydrogen exchange (HX) with protons from the solvent. Generally, NMR experiments using the out-and-back coherence transfer with amide proton detection are affected by fast HX and result in reduced signal intensity. When one of these experiments, 1H-15N HSQC, is used to measure the 15N transverse relaxation rate (R2), the measured R2 rate is convoluted with the HX rate (kHX) and has higher apparent R2 values. We demonstrate this effect by performing 15N R2

CPMG experiments on α-synuclein, an intrinsically disordered protein (IDP). In conclusion, various sources for HX effect on R2

CPMG experiments are described and the HX effect can be corrected by a derived equation and the steady state pulse.

Poster 032 Measurement of Flap Conformational Sampling and

Binding Interaction Changes of HIV-1 Protease Variants Xi Huang1; Angelo Veloro1; Mandy Blackburn2; Gail Fanucci1; 1Department of Chemistry, University of Florida, Gainesville,

FL; 2University of Massachusetts, Amherst, MA Double electron-electron resonance (DEER) has been used to show that sequence variations in HIV-1 protease (HIV-1PR) subtypes result in different average flap conformational ensembles. Inhibitor binding is shown to induces shifts in flap conformational sampling. 15N-HSQC titration methods are used to estimate inhibitor binding strength by observing changes in the NMR peak patterns. Because DEER data are collected at 65K, here, we use solution NMR to confirm DEER results. The HSQC titration results support the results of DEER and suggest that it can be used to study highly dynamic enzyme system such as HIV-1PR upon interaction with inhibitors and substrates.

Poster 033 Solution NMR Insights into the Blue/Green Light

Absorbing States of an Active Cyanochrome Domain Containing a Double Linked PCB Chromophore

Gabriel Cornilescu1; Claudia C. Cornilescu1; Andrew T. Ulijasz2; Joseph M. Walker1; Richard D. Vierstra1; John L. Markley1; 1University of Wisconsin-Madison, Madison, WI;

2University of Wisconsin–Milwaukee, Milwaukee, WI A novel class of Phy-like chromoproteins discovered in cyanobacteria (designated as cyanochromes) photoconvert between stable blue (Pb) and green light-absorbing (Pg) forms. The GAF domain of Thermosynechococcus elongatus (Te-PixJ GAF) is particularly amenable to spectroscopic studies, because photoconversion of the Pb form to the Pg is complete, making it possible to investigate both forms in isolation. These distinctive absorption properties are associated with the binding of phycocyanobilin (PCB) via two stable cysteine-based thioether linkages within the GAF domain. NMR data show that the protein undergoes considerable global structural changes upon photoconversion between Pb and Pg. We describe properties of the protein residues surrounding the chromophore and the conformational changes of both protein and chromophore upon photoconversion between Pb and Pg.

Poster 034

NMR Solution Structure of Opa60: A Neisserial Membrane Protein that Mediates Host Phagocytosis

Daniel Fox; Linda Columbus; University of Virginia, Charlottesville, VA

Opa proteins from the Neisseria genus are outer membrane proteins that induce human cells to engulf the bacterium. The receptor engaged by Opa proteins depends on the sequence of two highly variable extracellular loops. To investigate the molecular determinants of Opa-receptor interactions, the NMR solution structure was determined. A variety of approaches were required to assign the different domains of Opa60. The β-barrel remains largely unperturbed after removing the loops with protease and reduced significant spectral overlap. Peptides corresponding to the highly dynamic regions were synthesized, reducing line broadening and allowing unambiguous assignment. The NMR solution structure reveals that Opa60 is a canonical eight-stranded β-barrel and the hypervariable loops are disordered and highly dynamic.

Poster 035

Structural Studies of the Shortened Fragment of the WT Beta-amyloid Peptide and Its Effects of Various

Orthomolecular Species Sandra Chimon Peszek; DePaul University, Chicago, IL

Great interest is focused on the “hair-pin” region, between residues 16 and 21 also known as the “KLVFFA” region. In spite of the growing importance of these intermediates as a therapeutic target for AD, there is little structural information about the intermediates of the shorter region between resides 22 and 35, Aβ(22-35), because of their non-crystalline and unstable nature. The primary objective of this study is to determine the structure of the hair-pin region of these interval sites without the presence of the “KLVFFA” residues. The examination of the shorter fragment at various stages of its misfolding will be examined along with the effects of orthomoleular / homeopathic species.



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Poster 036 Characterization of Structure and Dynamics in Spider Silk

with 2H-13C Correlation NMR Experiments Xiangyan Shi; Gregory P. Holland; Jeffery L. Yarger;

Department of Chemistry and Biochemistry, ASU, Tempe, AZ Deuterium NMR line shapes and spin lattice (T1) relaxation times are very sensitive to local molecular motion and structure. This can be used to determine the dynamics and structure of proteins and biopolymers. However, conventional one-dimensional (1D) 2H NMR line shapes can be limited for dynamic studies of complex biomolecules due to the large quadrupolar coupling interaction compared with a small chemical shift window. In this study, two-dimensional (2D) 2H-13C HETCOR NMR experiments and 13C-detected 2H T1 relaxation measurements are used to probe the local, site-specific molecular dynamics of various secondary structural elements in spider silk fibers.

Poster 037

Structural Analysis of the C-Terminus of Lung Surfactant Protein B

Anna Kuznetsova1, 2; Julieann Vanni2; Joanna Long2; 1Chemistry Department, University of Florida, Gainesville, FL;

2Department of Biochemistry, University of Florida, Gainesville, FL

Using ssNMR we determined that helical C-terminus of surfactant protein B (SPB59-80) penetrates deeply into 4:1DPPC:POPG lipid bilayers and binds more peripherally to 3:1POPC:POPG bilayers. This differential partitioning provides insight into breathing mechanism. Deep penetration within DPPC:POPG bilayers requires the charged peptide sidechains to “snorkel” to interact with charged phosphate headgroups and the actual torsion angles may deviate from those expected for canonical a-helix. We are using solution NMR data to determine SPB59-80 conformation in a highly curved lipid mimetic environment of detergent micelles and to compare to helical conformations of SPB59-80 in lipid bilayers obtained with MAS ssNMR homonuclear recoupling experiments. Power saturation EPR is used to evaluate peptide conformations and each residue penetration depth in all environments.

Poster 038

Conformational Flexibility and Binding Promiscuityin CD46 Complement Protein

Devon Sheppard; University of Oxford, Oxford, UK Complement protein CD46 is a multidomain, transmembrane protein which acts as a cofactor in the degradation of C3b and C4b. In addition to its interaction with other complement proteins, the first two CCP (Complement Control Protein) domains are bound by a number of human pathogens. Available crystal structures for the CD46 demonstrate a broad distribution for the angular relationship between these first two domains, resulting in a ligand specific binding interface. The CCP are proline rich and disulphide bonded with a low degree of secondary structure and high degree of solvent accesibility. 15N relaxation analysis in conjunction with deuterium exchange of a CCP1and CCP2 construct provide a dynamic profile for these domains for a broad time scale.

Poster 039 Structural Studies of the Glycosaminoglycan Binding Proteins and Chondroitin Sulfates Interaction by NMR Younghee Park; CCRC, University of Georgia, Athens, GA

The Link-TSG-6 and CCL5 proteins are well known to bind glycosaminoglycans contributing to the formation and stability of the extracellular matrix during the inflammation and activating leukocytes through receptors, respectively. Several chondroitin sulfate (CS) oligomers with and without a spin label at the reducing end are used to study interactions studies with these proteins. These studies are supported by chemical shift perturbations in 1H-15N-HSQC spectra leading to the identification of several residues involved in binding for both Link-TSG-6 and CCL5. Also, RDC experiments suggest minimal conformational changes on CS binding. STD experiments were carried out to identify contact sites on the CS oligomers.

Poster 040

Ultrahigh Resolution MAS NMR Studies of Structure and Dynamics in HIV-1 Capsid Protein Assemblies

Yun Han1, 2; Christopher Suiter1, 2; Guangjin Hou1, 2; Jinwoo Ahn2; In-Ja Byeon2; Andrew Lipton3; Sarah Burton3; Ivan

Hung4; Peter Gor'kov4; Zhehong Gan4; William Brey4; David Rice5; Angela Gronenborn2; Tatyana Polenova1, 2; 1University of Delaware, Newark, DE; 2University of Pittsburgh School of

Medicine, Pittsburgh, PA; 3Pacific Northwest National Laboratory, Richland, WA; 4National High Magnetic Field Laboratory, Tallahassee, FL; 5Agilent Technologies, Inc.,

Santa Clara, CA We present recent progress towards obtaining atomic-level structural and dynamics information on protein assemblies involved in two key steps of the human immunodeficiency virus 1 (HIV-1) viral lifecycle, capsid assembly and viral maturation. We demonstrate that tubular assemblies of HIV-1 capsid (CA) and capsid-spacer peptide 1 (CA-SP1) proteins yield unprecedented high-quality homo- and heteronuclear MAS NMR correlation spectra at ultrahigh magnetic fields, enabling their structural and dynamics investigations at atomic resolution.

Poster 041

EVO2: An Improved Version of Projection Decomposition Analysis

Jonas Fredriksson1; Martin Billeter2; Fabio C.L. Almeida1; 1Centro Nacional de Ressonância Magnética Nuclear, Rio De Janeiro, Brazil; 2University of Gothenburg, Goteborg, Sweden Projection experiments for protein characterization are beneficial due to both the substantial time saving and the resolution gain when observing several nuclei but recording in two dimensions only. Several procedures have been proposed for the processing of projections. We present an improved algorithm called EVO2 that solves an over-determined equation system using peaks from all projection experiments as input. From a systematic analysis of combinations of peak sets, the final solution is selected on the basis of lowest residual. Novel features include the handling of convoluted projections, a wider range of experiments and a graphical user interface including improved correlation calculations and sequential positioning to provide a complete description of the protein. An example is given for the defensin HBD6.



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Poster 042 Characterization of RNA Dynamic Ensemble using NMR

RDCs and Topologically Allowed Space Shan Yang; University of Michigan, Ann Arbor, MI

Nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) can provide a unique way to characterize the motions of RNA with timescale extended up to milliseconds. Recent developed domain-elongation method makes it possible to decouple the overall tumbling and inter-helical motions of RNA which allows exclusive interpretation of the inter-helical motions using RDCs. Here, we present an approach, Sample and select (SAS), for constructing ensemble of structures which represent the dynamics of elongated RNAs from a predefined and uniformly sampled topologically allowed structure space by fitting the RDCs. With this approach, inter-helical dynamics of several RNAs including the previously studied HIV-1 TAR and HIV-2 TAR are successfully characterized.

Poster 043 Domain Cooperativity of Multidomain Proteins

Investigated by RDCs: What Can We Learn from Molecular Alignment in Anisotropic Media?

Tairan Yuwen; Carol B. Post; Nikolai R. Skrynnikov; Purdue University, West Lafayette, IN

We seek to characterize spatial cooperativity of domains in multidomain proteins by measuring their alignment in weakly orienting media. A number of constructs consisting of two α-spectrin SH3 domains connected by a flexible Gly/Ser linker have been prepared. These chimera proteins were dissolved in PEG/hexanol media, allowing for collection of RDC data. As expected, the degree of protein alignment decreases with increase in the length of the linker. These results have been supported by in silico PALES-based simulations. At the same time, we cannot explain high degree of alignment observed in an isolated SH3 domain. Further progress in this area depends on our ability to understand the details of alignment mechanism and develop the appropriate modeling tools.

Poster 044

Calmodulin Complexed to An N-terminally Acetylated α-Synuclein Peptide

James Gruschus; Thai Leong Yap; Jennifer C. Lee; Laboratory of Molecular Biophysics, Bethesda, MD

Calmodulin (CaM) is a calcium binding protein that plays numerous roles in Ca-dependent cellular processes, including uptake and release of neurotransmitters in neurons. α-Synuclein (α-syn), one of the most abundant proteins in neurons, helps maintain presynaptic vesicles containing neurotransmitters and moderates their Ca-dependent release. Ca-bound CaM interacts with α-syn at several locations along its sequence, with the strongest interaction seen at the N-terminus. In contrast, Ca-free CaM has negligible interaction. In neurons, most α-syn is acetylated at the N-terminus, hence we chose to study the complex with an N-terminally acetylated α-syn peptide containing the first 19 residues. The acetylated peptide adopts a helical structure when bound. Unexpectedly, even when unbound, it retains some helical character compared to full-length, non-acetylated α-syn.

Poster 045

Motions on the Millisecond Timescale and Multiple Conformations of HIV-1 Capsid Protein: Implications for

Structural Polymorphism of CA Assemblies

Guangjin Hou1, 2; In-Ja Byeon2, 3; Yun Han1, 2; Christopher Suiter1, 2; Jinwoo Ahn2, 3; Jinwon Jung2, 3; Chang-Hyeock Byeon2, 3; Angela Gronenborn2, 3; Tatyana Polenova1, 2;

1University of Delaware, Newark, DE; 2Pittsburgh Center for HIV Protein Interactions, Pittsburgh, PA; 3University of

Pittsburgh School of Medicine, Pittsburgh, PA The capsid protein (CA) of human immunodeficiency virus 1 (HIV-1) assembles into a cone-like structure that encloses the viral RNA genome. Interestingly, significant heterogeneity in shape and organization of capsids can be observed in mature HIV-1 virions. In vitro, CA also exhibits structural polymorphism and can assemble into various morphologies, such as cones, tubes and spheres. Here we investigate the origin of CA structural plasticity using solid-state and solution NMR spectroscopy. In the solid-state, the hinge region connecting the NTD and CTD is flexible on the millisecond timescales, allowing the protein to access multiple conformations, essential for pleomorphic capsid assembly. In solution, the CTD dimer exists in two major conformations, whose relative populations differ for different length CTD constructs.

Poster 046

Defining a Near Native Hydrated Intermediate of Calmodulin by 19F NMR and 1H Spin Diffusion

Experiments Sacha Larda; University of Toronto, Mississauga, Canada

Calmodulin (CaM) is a 148 residue calcium sensor serving as a signaling hub for a variety of cellular pathways. The protein consists of four EF-hand motifs, separated by a flexible alpha-helix. While 15N,1H spectra do not indicate the presence of a folding intermediate, 19F NMR studies, using fluoro-Phe as a probe, reveal that CaM undergoes a transition to a near native hydrated state around 50C. 19F CPMG studies provide a measure of the rate of fluctuation between native and near native states, which is generally around 11 kHz at 55C. In this study, we employ 15N,1H HSQC-detected 1H spin diffusion experiments to delineate the transition between the native state and the near-native hydrated state and obtain reliable estimates of populations.

Poster 047

Studies of Oligomeric State and Dynamics of Conformational Exchange of a Small Multidrug

Transporter, EmrE Supratik Dutta; Washington University School of Medicine, St.

Louis, MO EmrE is a member of small multidrug resistance (SMR) family, found in the inner membrane of Escherichia coli. It extrudes polyaromatic cations from the bacterial cytoplasm by H+-coupled transport. EmrE is a dimer where each monomer contains four transmembrane helices. Our data indicates that the oligomerization of EmrE is lipid dependent and the monomer-dimer dissociation constant is ~10 μM in 56 mM lipid for apo-protein. In order to perform transport, conformational exchange of monomers within the dimer is important. The preliminary SM FRET results show the conformational exchange is 100-200 msec at 25ºC. Currently the analyses of fast dynamics (R1, R2, and HetNOE) NMR experiments are underway to refine the current structure of EmrE and compliment the slow dynamics results.



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Poster 048 Analysis of Conformational Sampling, Flexibility and Protein-Inhibitor Interaction Dynamics of a Multi-drug

Resistant HIV-1 Protease Variant Ian Mitchelle De Vera; Mandy Blackburn; Ben Dunn; Gail

Fanucci; University of Florida, Gainesville, FL In this study, HIV-1PR samples of the multi-drug resistant clinical isolate MDR 769 bound to nine FDA-approved protease inhibitors and a non-hydrolyzable substrate mimic were analyzed by 1H-15N heteronuclear single quantum coherence (HSQC) to study protein-ligand interaction dynamics. Pulsed electron paramagnetic resonance (EPR) data were also collected to determine inhibitor-induced conformational sampling shifts. NMR relaxation measurements (T1, T2 and 15N NOE) were employed to compare backbone dynamics of MDR 769 to subtype B. Results show that higher DEER percentage closed population coincides with higher estimated inhibitor or substrate residence time and binding strength from HSQC titration data. This shows that DEER results obtained for MDR 769 at cryogenic conditions (65 K) are corroborated by ligand-protein interactions observed in solution.

Poster 049

Exploring the Molecular Basis for Antibiotic Resistance via Paramagnetic Relaxation Enhancement

Thomas Frederick; V N Sivanandam; Daniel Mulhall; Brian Wilson; Jeffrey Peng; Univ of Notre Dame, Notre Dame, IN

BlaR1 is a β-lactam sensor protein that confers broad-spectrum antibiotic resistance to bacteria by regulating the production of β-lactamase enzymes that destroy penicillin-like antibiotics. Antibiotic binding to the extracellular BlaR1 sensor domain (BlaRs) initiates a transmembrane signal transduction process. This process is poorly understood; it is believed to involve an interaction between extracellular loop L2 and BlaRs. We used paramagnetic relaxation enhancement (PRE) to characterize the interaction between a peptide mimic of L2 and BlaRs. Our results suggest that L2short interacts with BlaRS in two locations. Preliminary 15N relaxation data suggest this result may reflect a monomer-dimer equilibrium of BlaRs. Relaxation analysis of 15N-labeled L2short corroborates the PRE results. Together, these data support the hypothesis of a critical L2/BlaRs interaction.

Poster 050

Structural and Dynamic Changes in Human β-defensins 1 and 6 upon Breast Cancer Cell Membrane Interaction Viviane Silva De Paula; Luize Lima; Robson de Queiroz

Monteiro; Fabio C.L. Almeida; Ana Paula Valente; Federal University of Rio de Janeiro, Rio De Janeiro, Brazil

The aim of this work is to characterize by NMR the interaction of human β-defensins (1 and 6) with: (i) microvesicles (MV) budded by breast cancer cells (cell lines MCF-7 and MDA-MB-231) and (ii) membrane models containing phosphatidylserine (PS), searching for correlations among immunological and binding properties of defensins. NMR analyses illustrated strong interaction with MCF-7, but only weakly with MDA-MB-231, suggesting an opposite correlation with the invasiveness of the cell. HbD6 made specific contacts with MCF-7 that were partially reverted by Annexin V, indicating that the interaction also involved other receptor besides PS. The weak interaction with metastatic cell

indicates a link between innate/adaptive immune responses and a possible mechanism in which cancer cells elude destruction and promote tumorigenesis.

Poster 051

31P and 1H NMR Methods for Detection and Quantification of Endoribonuclease Activity

Christina Mozes; Daniella Ishimaru; Mirko Hennig; Medical University of South Carolina, Charleston, SC

Endoribonucleases constitute a broad class of enzymes which regulate prokaryotic and eukaryotic gene expression through post-transcriptional pathways, including mRNA turnover. Frequently, catalysis employs the two-step mechanism of transesterification and hydrolysis, where the first reaction results in cleavage of the RNA substrate and generation of a 2’,3’-cyclic phosphate on the 5’ product. Subsequent hydrolysis proceeds more slowly, resulting in accumulation of the cyclic phosphate intermediate. Here we report 1H and 31P spectroscopic methods for detecting the 2’,3’-cyclic phosphate signature of endoribonuclease cleavage and determining enzymatic rates. Scalar 2J2’/3’CP and 3J2’/3’HP values are reported. This straightforward routine simplifies characterization of endoribunucleases, whose activity has been underestimated in the past due to difficult detection and the prominence of exonuclease mRNA decay pathways.

Poster 052

Solution and Solid State NMR Analysis of Model Proline Containing Peptides Mimicking β-turn Structures

S. Raghothama; Indian Institute of Science, Bangalore, India Rationale design of peptide sequences taking up cis conformation could be realized by use of pseudo-proline. We focus here on solution and solid state NMR analysis of tripeptide Piv-DPro-§Pro-Leu-NHMe along with similar peptides. The cis form in solution could be established by diagnostic NOEs. Solid state 13C CPMAS showed two set of resonances with 50:50 ratio. Majority of 40 odd resonances could be assigned using spectral editing techniques followed by hector correlations at natural abundance. With the help of recently development hector double quantum correlation experiments we were able to get some structural insights in solid state which could correspond to coexisting cis / trans forms. SSNMR would be a good substitute to provide information similar to crystal structure.

Poster 053

Application of NMR and EPR Methods to the Measurement of Homodimer Subunit Exchange Rates

Yunhuang Yang; Department of Chemistry and Biochemistry, Miami Un, Oxford, OH

Paramagnetic relaxation enhancement (PRE) measurements and pulsed electron paramagnetic resonance - double electron-electron resonance (DEER) experiments have been widely applied to protein structure determination, protein dynamics studies, and to characterization of homodimer protein complex structures. Here we extend the application of PRE and DEER to direct measurement of homodimer subunit chain exchange rates. The method was demonstrated by monitoring subunit chain exchange in a MTSL spin labeled Dsy0195 homodimer. By fitting the DEER spectra intensity changes during sample mixing, a homodimer subunit exchange rate about 17.9 min-1 was derived. Independent PRE measurements resulted in an average exchange rate of



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21.3 min-1 consistent with the DEER experiment result. These methods can be applied to protein-protein, or protein-DNA exchange studies.

Poster 054

Characterization of 5-Hydroxy-2'-Deoxycytidine Based Paired With 2'-Deoxyguanosine In DNA

Marta Szulik1; Manjori Ganguly2; Patrick Donahue1; Kate Clancy2; Barry Gold2; Michael Stone1; 1Vanderbilt University,

Nashville, TN; 2University of Pittsburgh, Pittsburgh, PA Incorporation of 5-hydroxy-2'-deoxycytidine (5-OH-dC) into DNA leads to C to T transitions. It is repaired by DNA glycosylases that require the base to be extrahelical in order to be excised from the DNA. Our thermodynamic and high-resolution NMR results describe the effect of a 5-hydroxy-2'-deoxycytidine•2'-deoxyguanosine base pair on the stability of DNA. NMR spectroscopy as a function of temperature reveals that base pairs at the modification site undergo increased exchange of their imino protons with solvent. Base stacking is maintained throughout the duplex. The results demonstrate that the lesion is destabilizing and the energy barrier for the "flipping" of 5-hydroxy-2'-deoxycytidine from DNA is lowered. This could provide a thermodynamic mode of adduct identification by repair enzymes.

Poster 055

Nuclear Magnetic Resonance (NMR) Studies of NADH Oxidase (NOX), a 54kDa Enzyme

Teresa Miletti; Anthony K Mittermaier; McGill University, Montreal, Canada

NADH oxidase (NOX) from the thermophile Thermus thermophilus is stable at high temperatures, but exhibits low activity below 70°C. NOX catalytic activity increases ~7-fold when the temperature is raised from 20 to 65 °C, and ~2.5-fold when small amounts of denaturant are added. Using NMR, we investigated temperature and urea dependence of NOX structure and dynamics. NOX has a structurally very stable core indicated by slow H/D-exchange. Broadening from microsecond-timescale motions was measured by a suite of novel 15N relaxation experiments. Nanosecond-picosecond motions were characterized by 15N relaxation measurements. Certain peaks show anomalous shifts in position in temperature and urea titrations, suggestive of conformational rearrangements. These results agree with previous studies implicating active-site dynamics in NOX catalytic activity.

Poster 056

Structural Studies of the Shortened Fragment of the Various Single Point Mutations of the beta-amyloid

Peptide Alvin Kang; DePaul University, Chicago, IL

A shorter (22-35) amino acid sequence is of interest due to the hair-pin turn, the exclusion of the amino acid region KLVFFA. The effect of fibril formation without the KLVFFA suggest that the hair-pin turn is an intermolecular hydrophobic core and is not needed for fibril formation. 5% of AD is caused by a missense mutation, in an inherited gene, and are capable of forming intramolecular and intermolecular beta-sheets. The single point mutations demonstrate varied rates of β-sheet formation compared to the wild type The obtained structures will be compared to those of the WT Aβ intermediates and fibrils, based on a hypothesis that the

molecular level structural change caused by the mutation also change the kinetics of misfolding.

Poster 057 Structural studies of a Hyperthermophilic Intein

Precursor Protein from DNA Polymerase II of Pyrococcus abyssi

Wen Chen; Rensselaer Polytechnic Institute, Troy, NY Protein splicing is a self-catalyzed and spontaneous post-translational process in which inteins excise themselves out of precursor proteins while the exteins are ligated together. We report the first discovery of an intramolecular disulfide bond between the two active-site cysteines, Cys1 and Cys+1, in an intein precursor composed of the hyperthermophilic Pyrococcus abyssi (Pab) PolII intein and extein. Protein splicing proceeds through a four-step reaction but the catalytic mechanism is not fully understood at the atomic level. With the help of our recent structure of Pab PolII intein itself and the intramolecular disulfide bond, the structure of Pab PolII intein precursor will be determined for the first time for intein precursor with native sequence, unveiling intein splicing mechanism.

Poster 058

Structural Insights into the Role of PHD Fingers in the MOZ and HBO1 HATs

Karen Glass1; Nehme Saksouk2; Pedro Pena3; Tiffany Hung4; Mukta Ullah5; Xiang-Jiao Yang5; Jacques Cote2; Or Gozani4;

Tatiana Kutateladze3; 1Albany College of Pharmacy, Colchester, VT; 2Laval University Cancer Research Center, Québec City, Canada; 3University of Colorado at Denver, Denver, CO; 4Stanford University, Stanford, CA; 5McGill

University, Montreal, Canada The MOZ and HBO1 histone acetyltransferases (HATs) are important for regulation of many cellular processes. They form multi-subunit complexes and contain several plant-homeodomains (PHD). PHD fingers recognize post-transcriptional modifications (PTMs) on the histone H3 tail, particularly tri-methylation at lysine 4 (H3K4me3). Current research indicates PHD fingers are divided into functional classes that bind other PTMs as well. Individual subunits within MOZ and HBO1 HATs harbor PHD fingers, however, their functional role has not been determined. We aim to elucidate the different substrate specificity and function of PHD fingers within MOZ and HBO1 towards histone tails using X-ray crystallography, NMR, fluorescence spectroscopy and mutagenesis. This will link recognition of the histone code to the regulation of HAT activity and chromatin remodeling.

Poster 059

Brazzein Active Site Tyr11/Tyr8 Lock in Distinct Conformations at Low Temperature

Claudia Cornilescu; Gabriel Cornilescu; Sarah F. Porter; Marco Tonelli; John L. Markley; Fariba M. Assadi-Porter;

University of Wisconsin-Madison, Madison, WI Brazzein, the smallest (54 residues) and one of the sweetest protein known so far, a remarkably heat stable and water-soluble, was originally isolated from the West African fruit of the climbing plant Oubli (Pentadiplandra brazzeana Baillon). We solved the solution structures at 3 °C and 37 °C of the recombinant brazzein, the ‘sweeter version’ of the wild-type, in which two tyrosines belonging to the ‘sweetness loop’ change



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significantly their orientation and hydrogen bond partners, resulting in distinct structures for this small thermostable protein. Modulating the strength of a pair of central disulfide bonds through the Tyr11/Tyr8 H-bonding may constitute a mechanism of interaction with sweetness receptors.

Poster 060

Human MRG15 uses the Chromodomain and the MRG Domain to Interact with the Methylated Histone Tail Xiaobai Ren1; Bartlomiej Blus2; Jaya Bhattacharyya1; Sepideh Khorasanizadeh1; 1Sanford-Burnham Medical

Research Institute, Orlando, FL; 2Laboratory of Cell Biology, Rockefeller University, New York, NY

Members of the Morf-related gene (MRG) family are subunits in histone acetyltranserase (HAT) and histone deacetylase (HDAC) complexes that occupy the transcriptionally-active regions in all eukaryotic genomes for epigenetic regulations. We studied the structure and function of a MRG protein conserved from yeast to human called MRG15. The human MRG15 is significant for RNA splicing, DNA repair, and general chromatin remodeling necessary for normal development. MRG15 contains 323 amino acids featuring an N-terminal chromodomain (a methyllysine-binding module) and a C-terminal MRG domain (a peptide-interacting module) linked by a flexible hinge. We discovered the histone peptide specificities for the MRG15 domains. Using NMR spectroscopy, we determined the molecular bases for the interactions of the MRG15 domains with partner histone peptides.

BIOMOLECULES, 061 - 069

Poster 061 Solution NMR Structure of REV1 C-terminal Domain and

Its Complex with Polh peptide Alexandra Pozhidaeva; Yulia Pustovalova; Irina Bezsonova; Dmitry Korzhnev; UCONN Health Center, Farmington, CT

REV1 is a Translesion Synthesis (TLS) DNA polymerase that plays a critical role in bypass replication across sites of DNA damage. Active sites of high-fidelity replicative DNA polymerases cannot accommodate most types of DNA damage. Therefore, in the process of TLS they are temporarily replaced by error-prone TLS enzymes that can successfully bypass DNA lesions thus allowing replication to continue. We used NMR spectroscopy to determine spatial structure of human REV1 C-terminal domain (REV1-CTD) and its complex with a peptide from Y-family DNA polymerase Polh. The determined structures revealed a universal mechanism of interaction of Y-family polymerases, including Polh, Polk and Poli, with REV1 protein, which provides a scaffold for assembly of multi-protein complexes carrying out bypass replication.

Poster 062

Natural Abundance Biomolecular NMR using Nanomole Quantities for the Analysis and Structure of Marine

Natural Products Frank Mari; Fred Pflueger; Sanaz Dovell; Helena Matei; Aldo

Franco; Florida Atlantic University, Boca Raton, FL NMR spectroscopy of limited quantities of sample (nanomolar or picomolar) is a challenge. Our laboratory studies peptidic marine natural products and typically, after a laborious

separation procedure, limited quantities of sample are obtained. The first step of our peptidomic screening is the evaluation of fractions by nanoNMR spectroscopy using methods developed in-house, which allows us to assess purity, quantity and the identification of diagnostic signals. In favorable cases, we can obtain the 3D structure of these peptides, including the determination of the disulfide pairing in constrained peptides. The limits of detection and other analytical parameters associated with these nanoNMR methods are evaluated. Several structures of venom-isolated peptides determined using nanoNMR methods will be presented.

Poster 063

Preliminary 13C, 2H NMR Studies of Serine and Water Dynamics in N.Clavipes Dragline Silk

Obehi Ukpebor1, 2; Anup Shah2; Emmanuel Bazov2; Gregory Boutis3; 1Hunter College of CUNY, New York, NY; 2Brooklyn

College Dept of Physics, Brooklyn , New York; 3Brooklyn College/CUNY, Brooklyn, NY

In this poster, we highlight results from a preliminary 13C and 2H NMR study on Nephila Clavipes silk fibers. Our current focus is on the thermal properties of the serine residues, and dynamics of water. Molecular dynamics based simulation studies of [GPGSG]5 mimetic peptide, indicate an inverse temperature transition similar to that of elastin as the temperature is raised from 20 to 40C. Simulations show evidence of an increase in sidechain contacts and peptide hydrogen bonds, concomitant with a decrease in localized water over a temperature range of 5C to 40C. Using deuterium 2D T1-T2 NMR, we studied the dynamics of water in the silk as a function of temperature; our data seem to qualitatively agree with our simulation findings.

Poster 064

Allosteric Effectors Interference: Functional Consequences and Structural and Dynamic Effects in

Hemoglobin Yue Yuan; Virgil Simplaceanu; Chien Ho; Carnegie Mellon

University, Pittsburgh, PA In the 'stripped' condition, hemoglobin exhibits a very high affinity for oxygen, while adding ions like chloride, phosphate, organic phosphates or hydrogen ions (lowering the pH) causes a decrease in the affinity. We show that in certain cases the allosteric effectors have a negative interference, i.e. while each effector separately causes a decrease in the affinity, when combined they partially negate each other's effect and the affinity increases. NMR experiments illustrate effects on the structure and dynamics of the subunit interfaces.

Poster 065

NMR Studies of Interactions Between Mutagenic Translesion Synthesis DNA Polymerases

REV1, polη and polζ Yulia Pustovalova; Alexandra Pozhidaeva; Dmitry Korzhnev;

UCONN Health Center, Farmington, CT REV1 is a mutagenic trans-lesion synthesis (TLS) DNA polymerase that enables replication across sites of DNA damage (lesions). The primary function of REV1 in TLS is to coordinate the concerted action of the other TLS polymerases with different DNA lesion specificity through specific protein-protein interactions. We use NMR spectroscopy to show that



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the C-terminal domain of REV1 has two independent binding sites for REV7 subunit of B-type polymerase ζ and Y-type polymerases η, κ and ι. This confirms a key role of REV1 in providing a binding platform for assembly of multi-protein complexes carrying out bypass replication across DNA lesions.

Poster 066

Probing Structure and Dynamics of an Artificially Generated Enzyme by Solution NMR

Fa-An Chao; Larry Masterson; Gianluigi Veglia; University of Minnesota, Minneapolis, MN

Starting from a known non-catalytic protein scaffold, we generated a novel RNA ligase by in vitro directed evolution. The enzyme evolved into a new fold containing little secondary structure, but retains its ability to coordinate two zinc ions. Based on H-X NOE and CPMG data, conformational dynamics are dramatically enhanced. Moreover, a double mutation designed to destabilize a zinc finger also increases enzyme activity by three-fold. Increases in fast and slow dynamics were identified at sites distal to the mutations. Remarkably, RDC data show little differences between the average conformations of wild-type and mutant proteins. These results highlight the prominent role of protein dynamics in enzyme design, suggesting a simultaneous evolution of structure and dynamics to achieve catalytic function.

Poster 067

Structural NMR Analysis of SK2 Potassium Channel Blocker Toxin-Like Peptides

Belen Ramírez-Cordero1; Patricia Cano-Sánchez1; Luis Brieba-de-Castro2; Federico del Río-Portilla1; 1Universidad Nacional Autonoma de Mexico, D.F., Mexico; 2Centro de

Investigación y de Estudios Avanzados, Irapuato, Guanajuato, Mexico

Tamapin (αKtx5.4), a toxin of the red scorpion Mesobuthus tamulus is the most potent and selective SK2 natural channel blocker. In this work we reported the structural determination using two-dimensional 1H-NMR of three peptides: r-tamapin, GS-tamapin and δN4L5-tamapin (δNL). The biosynthesis of all peptides was performed in E. coli rosetta gami, this strain left to obtain the peptides with their three native disulfide bridges. Experimental NMR structures confirmed tamapin how a member of αKTx5 subfamily. The addition of two residues (Gly-Ser) to the native sequence did not modify the secondary structure but gave a less active peptide. The deletion of asparagine 4 and leucine 5 provided an elongation in the α-helix motif what can enhance its blocker activity.

Poster 068

Mycobacterium Tuberculosis Membrane Protein Rv1861: Structural Studies of a Nucleotide Binding Protein in a

Native-Like Lipid Bilayer Environment Dylan Murray1, 2; Ivan Hung2; Timothy Cross1, 2; 1The Florida

State University, Tallahassee, FL; 2The National High Magnetic Field Laboratory, Tallahassee, FL

Today tuberculosis affects 1/3 of the worlds population. Rv1861 is a M. tuberculosis integral membrane protein likely involved in cell wall reorganization, a key step in the life cycle of the bacterium. The protein contains three transmembrane alpha helices and a nucleotide binding motif. Aligned sample and magic angle spinning NMR provide a path to structure

determination for integral membrane proteins in native-like environments. Here we present the characterization of the tilt and rotation angles for the three transmembrane alpha helices in Rv1861 derived from aligned sample SAMPI4 data. Additionally we present the initial assignments for isotropic chemical shifts derived from magic angle spinning correlation spectra.

Poster 069

High-Definition NMR Structure of PED/PEA-15 Death Effector Domain Allows Assessment of Key Side Chain

Interactions on the Protein Surface Edward Twomey1; Yufeng Wei1, 2; 1Seton Hall University, South Orange, NJ; 2Rockefeller University, New York, NY

PED/PEA-15 (phosphoprotein enriched in diabetes/astrocytes, 15 kD) is a small, non-catalytic, death-effector domain (DED) containing protein, that is widely expressed in different tissues and highly conserved among mammals. PED/PEA-15 has been found to interact with several protein targets in various pathways, and these targets include FADD and caspase-8 (apoptosis), ERK1/2 (cell cycle entry), and PLD1/2 (diabetes). We have recently refined the PED/PEA-15 DED structure with additional residual dipolar coupling (RDC) restraints measured from two independent alignment media using explicit solvent refinement protocol. The improved structural quality of the protein allows us to assess the charge triad interactions, together with several other functionally important surface interactions, which provide profound structural insights in the regulatory roles of PED/PEA-15 in various cellular processes.

CALCULATIONS & SIMULATION, 070 - 084

Poster 070

ARMOR: A Package for Accurate and Rapid Computation of Molecular Optimization Restraints

Konstantin Berlin; Nail A. Gumerov; Ramani Duraiswami; Kwaku Dayie; David Fushman; University of Maryland,

College Park, MD We present ARMOR (Accurate and Rapid computation of Molecular Optimization Restraints) package for rapidly computing several important long-range molecular restraints used in multi-domain structural refinement of complexes consisting of DNA, RNA, and/or proteins. The package consists of three major toolboxes: (i) a package for processing, prediction, and rigid-body docking based on nuclear spin-relaxation; (ii) a package for processing, prediction, and rigid-body docking based on Residual Dipolar Couplings; and (iii) a high-performance parallelized (CPU and GPU) package for prediction of Small-Angle Scattering profile. ARMOR can run on virtually any platform, including Linux, Windows, and Mac OS, and contains a highly scalable, thread-safe API that can be rapidly leveraged by advanced users for easy integration into their own software.

Poster 071

Assessment of the Dependence of Aromatic 13C Chemical Shifts on Conformation and Dynamics

Geoffrey A. Mueller1; Lalith Perera1; Wim Vranken2; Alexander Lockhart1; Robert London1; 1NIEHS/NIH, Research Triangle

Park, NC; 2Vrije Universiteit Brussels, Brussels, Belguim This study sought to examine the effect of structure and dynamics on the 13C shift of the Cdelta aromatic carbon in



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phenylalanine and tyrosine residues. Quantum mechanical calculations predict that the occluded conformation of the chi2 dihedral angle (0°) should shift the 13Cdelta average upfield by -1.6 ppm relative to the relaxed conformation (90°), with an additional more complex dependence on chi1. To evaluate the effect of dynamics on the 13Cdelta chemical shift, we considered a restricted diffusion model in which the aromatic group rotates ± theta degrees about chi2. This model predicts that the sign and magnitude of the chemical shift change depends on the initial value of chi2, and theta, which is a function of S2.

Poster 072 Peak Identification using Nonnegative Matrix

Decomposition in Hyper Dimensional NMR Spectra Suhas Tikole1; Victor Zharavin1; Peter Güntert1, 2; 1Institute of Biophysical Chemistry, BMRZ, Frankfurt am Main, Germany; 2Graduate School of Science, Tokyo Metropolitan University,

Hachioji, Tokyo, Japan Precise estimation of frequencies of peaks in NMR spectra is complicated by poor signal-to-noise ratio and overlap. This poses combinatorial ambiguity problems for signal assignments and increases errors in NOE distance restraints. To alleviate this problem, a more sophisticated peak decomposition algorithm, based on Nonnegative Matrix Factorization (NMF), was developed. In the automated peak picking approach a phase of peak identification is followed by estimation of peak intensities and frequencies. Several types of regularizations and divergences were used and their performances were compared. It also allows applying constraints if some information is known a priori, e.g. total number of peaks or positions in common dimensions of Hyper-Dimensional (HD) shapes.

Poster 073

Lowering NMR Data Requirements in Protein Structure Determination using REDCRAFT

Mikhail Simin; Paul Shealy; Homayoun Valafar; University of South Carolina, Columbia, SC

Our exploration of information content of RDC data strongly supports the possibility of structure determination from only two RDC data per residue. This investigation also covered structure determination from backbone { C-N, N-H, C-H } RDC data. Utilizing RDCs from this triplet is often considered challenging due to its planar atomic arrangement. Multiple computational features have been added to REDCRAFT to help achieve the above two objectives. We present structures computed from minimal experimental RDC data, as well as from planar backbone RDC data. Details of this investigation and discussion of our computational features will be presented.

Poster 074

Natural Bond Orbital Description of Unpaired Electron Spin: Molecular Dynamics Simulations Restrained by

Paramagnetic NMR Parameters of Hyperfine-shifted Signals

D. Flemming Hansen1, 4; William M. Westler2; Micha B. A. Kunze1; John L. Markley3; Frank Weinhold3; Jens J Led4; 1ISMB, University College London, London, UK; 2National

Magnetic Resonance Facility at Madison, Madison, WI; 3University of Wisconsin-Madison, Madison, WI; 4University of

Copenhagen, Copenhagen, Denmark

A natural bond orbital (NBO) analysis of unpaired electron spin density in metalloproteins is presented, which allows a fast and robust calculation of paramagnetic relaxation enhancements (PREs). Electron spin density in both metal-ligand and in local orbitals contributes to the PRE of heavy nuclei; we show how local NBOs of the relaxing nucleus can be used to calculate accurate PREs for 15N nuclei. The presented NBO formalism makes it computationally feasible to include experimental paramagnetic NMR parameters of 15N nuclei as restraints in molecular dynamics simulations. As an example, we present a restrained molecular dynamics simulation of the iron-sulphur protein rubredoxin, where experimental PREs and contact shifts of the hyperfine-shifted 15N nuclei are included as restraints using the NBO formalism.

Poster 075

Complete NMR Spectral Analysis in Automation Matthias Niemitz; Juuso Lehtivarjo; Samuli-Petrus Korhonen;

PERCH Solutions, Kuopio, Finland NMR parameters (chemical shifts and coupling constants) extracted from easily available 1H spectra provide comprehensive structural information. However, spectral overlap and higher order effects pose a challenge to retrieve these NMR parameters. Complete NMR spectral analysis using quantum mechanical optimization of NMR parameters matching the actual ones in the experimental data is the classic approach solving this problem. We present a highly automated procedure extracting NMR spectral parameters from 1H-spectra even with overlapping signals and higher order effects. HSQC and 13C information can also be utilized. Evaluating the similarity of the extracted spectral parameters to the predicted ones the procedure makes a safe assessment on the consistency between structural and spectral data with a minimum of false positive assignments.

Poster 076

Contribution of New Features of REDCAT in Study of Macromolecular Structure and Dynamics

Christopher Schmidt; Stephanie Irausquin; Homayoun Valafar; University of South Carolina, Columbia, SC

Protein motion on a biologically relevant time scale has becoming increasingly important in the creation of pharmaceutical agents. RDCs are the only source of NMR data that describes this motion for macromolecular structures. However, their elusive nature complicate their utility and introduces challenges in their analyses. Recent experiments were performed in order to assess the ability of REsidual Dipolar Coupling Analysis Tool (REDCAT) to identify mobile regions within a protein, and categorizes correct models of dynamic for these regions utilizing multiple alignment media. One such target for pharmaceutical research is human Thymidylate Synthase (hTS). Two known mobile domains undergo internal dynamics as an important part of its biological function. Here, these results and further enhancements to REDCAT will be presented.

Poster 077

A New Automatic Baseline Correction Method Bao Qingjia1; Chaoyang Liu1; Fang Chen2; 1Huazhong University of Science and Technology, Wuhan, China;

2Wuhan Institute of Physics and Mathematics, Wuhan, China



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A new automatic baseline correction method for NMR spectra is presented. It is based on an improved baseline recognition method and a new iterative baseline modeling method. The experimental results indicate our new baseline correction method is more effective for processing NMR spectra with severe baseline distortions

Poster 078

Copper-cationic Dummy Atom Molecules Applied to Aβ(1-40) and Superoxide Dismutase Systems in Molecular

Dynamic Simulations Dan McElheny; Sudhakar Parthasarathy ; Yoshitaka Ishii;

University of Illinois at Chicago, Chicago, IL Accurate and efficient molecular dynamic simulations of metalloenzymes are a challenging task. Here we present a copper-cationic dummy atom approach which is easily implemented into molecular mechanical force fields such as AMBER. The method is readily applied to nanosecond length simulations for study of interactions between Cu2+ and its ligands. Also of note is the ability to build Cu2+ models which serve as a mimetic for either tetrahedral or square-planar complexes without the need for covalent bonds or harmonic restraints imposed onto the copper complex. Here we report simulations used to help interpret 13C SSNMR signal quenching results obtained for Cu2+ /Aβ(1-40) complexes. Findings for water entry into the active site for Cu, Zn Superoxide Dismutase will also be presented.

Poster 079

Self-assembly of Organic Functionalized Materials through Hydrogen Bonding and Dispersion Forces from

First Principles and solid-state NMR Dmytro Dudenko1; Martin Wegner1; Luis Mafra2; Jie Shu1;

Robert Graf1; Michael Ryan Hansen1; Hans Wolfgang Spiess1; 1Max-Planck-Institute for Polymer Research, Mainz,

Germany; 2Chemistry Department,CICECO,University of Aveiro, Aveiro, Portugal

The control of the local molecular packing and the design of tailored supramolecular ordered nanostructures is one of the key challenges for the rational design of novel functional materials with unique mechanical, electronic, pharmaceutical, and biological properties. The self-assembly of these systems is accomplished by a delicate balance of attractive forces between individual molecules, such as hydrogen bonding, or van der Waals interactions. Solid-state NMR experiments and extensive Car-Parrinello Molecular Dynamics (CPMD) simulations together with Nuclear Independent Chemical Shift (NICS) can be used to gain deeper insight into supramolecular self-organization. We demonstrate the potential of NMR methods in helical supramolecular systems and different forms of antibiotic drugs where up to 50 carbon and proton sites could be distinguished.

Poster 080

You Spin Me Right Round: Tensors and Rotations in NMR

Leonard J Mueller; University of California, Riverside, Riverside, CA

The transformation of second-rank Cartesian tensors under rotation plays a fundamental role in the theoretical description of nuclear magnetic resonance experiments. Two approaches to treating rotation are the direct transformation of the spatial tensor in Cartesian form and the decomposition of

the tensor into irreducible spherical tensor components that rotate in subgroups of rank 0, 1, and 2. While these two approaches must give equivalent results, there is an apparent inconsistency in the NMR literature, where the rotation in spherical tensor form has typically been partnered with the inverse rotation in Cartesian form to produce equivalent transformations. Here, the origin of this discrepancy is shown and this surprising and longstanding inconsistency reconciled.

Poster 081

Chemometrics and NMR-Based Fingerprints Elena Demetrio; ACRAF, Pomezia - Roma, Italy

A large number of NMR spectra is daily produced in pharmaceutical analytical laboratories, but the information contained in the spectra is not fully exploited and often employed only for analytical purposes. Computer-aided drug design and in particular structure-based drug design can indeed benefit from the information collected through NMR spectroscopy. Following the ideas of Beger who introduced the methodology called Spectrometric Data-Activities Relationship (SDAR), we built molecular fingerprints from NMR spectral data of proprietary molecular libraries with the objective to develop new molecular representations that can describe the chemical space from a different perspective. The approach was successfully applied to two studies having relevant interest in the field of drug design.

Poster 082

nDh-PDPA: n Dimensional Hybrid Probability Density Profile Analysis

Arjang Fahim; Mikhail Simin; Homayoun Valafar; University of South Carolina, Columbia, SC

In an effort to expand the boundaries of NMR spectroscopy, the cost of structure determination of routine proteins has been neglected. Our lab has introduced Probability Density Profile Analysis (PDPA), a method to address the economics of structure determination of routine proteins and to identify novel structures from a minimal set of unassigned NMR data. Here we present our most recent development, n-Dimensional Hybrid Probability Density Profile Analysis (nDh-PDPA), that allows the inclusion of unassigned NMR data such as: RDC data from multiple vector types in multiple alignment media, rCSA, PRE, and pseudo contact shifts. nDh-PDPA, has reduced the needed computation time, while improving the sensitivity and selectivity compared to its predecessors simply by including data that are readily available.

Poster 083

Central Transition Lineshapes for Half-Integral Spins. Perturbation vs. Exact Solutions

Alex D. Bain; McMaster University, Hamilton, Canada We are familiar with the lineshape of the central transition of a spin perturbed to second-order by the quadrupole interaction. To first order, the transition is unaffected, and the second order formulae are well-known. Recently, we have been working on a direct method to calculate the spectra exactly, without any approximations [ A.D. Bain, B. Berno, Prog.Nucl.Magn.Reson.Spectrosc. 59 (2011) 223-244. 1]. This approach is important as we look at systems with large quadrupole couplings, but it also provides an alternate route to the perturbation results. In perturbation theory,



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transitions are perturbed by their mixing with other coherences, which changes their frequencies. The gives a clear physical picture of how the single quantum transitions are mixed with other coherence levels.

Poster 084

Software Tools for Biomolecular NMR Structure Determination

Charles Schwieters; National Institutes of Health, Bethesda, MD

We present new features and an overview of software packages developed and maintained in our group: Xplor-NIH and VMD-XPLOR. New features include improved facilities for modeling NMR/SAXS structure refinement of heterogeneous ensembles of structures, Bug fixes and enhancements to the Steric Alignment RDC potential term [J.-R. Huang and S. Grzesiek, JACS 132, 694 (2010)], and significant enhancements to the VMD-XPLOR visualization package

DETECTION, 085 - 087

Poster 085

Wireless Microsensors for Electron Paramagnetic Resonance Tooth Dosimetry

Barjor Gimi; Benjamin Williams; Harold Swartz; Dartmouth Medical School, Lebanon, NH

In order to effectively manage medical care following an event were many thousands of people may have been exposed to levels of radiation sufficient to cause acute radiation syndrome, new technology is needed to provide individual absorbed dose estimates. In vivo electron paramagnetic resonance (EPR) tooth biodosimetry is capable of providing such dose estimates based on quantitative measurement of the numbers of persistent free radicals generated in tooth enamel during irradiation. We have devised wireless microsensors for high-throughput EPR tooth biodosimetry. EPR spectra were acquired using a prototype of the biodosimeter operating at 40mT and 1150MHz. Use of the microcoil resulted in an increase in SNR compared to detection with the external coil directly.

Poster 086

Flow-based MRI and MR-EIT at Ultra-low Fields Per Magnelind1; Evgeny Burmistrov1; John George1; John

Gomez1; Andrei Matlashov1; Don Tucker2; Sergei Turovets3; Algis Urbaitis1; Petr Volegov1; Michelle A. Espy1; 1Los Alamos

National Laboratory, Los Alamos, NM; 2Electric Geodesics, Inc., Eugene, OR; 3Neuroinformatics Center, University of

Oregon, Eugene, OR SQUID-based detection of magnetic resonance in the kilohertz range has been shown to allow interleaved multi-modal imaging with anatomical ultra-low field (ULF) MRI and magnetoencephalography (MEG) providing functional information. Hemodynamic ULF imaging correlated to the same stimulus as the MEG could provide additional constraints for the MEG source localization, which is composed of an ill-posed problem. We will present FAIR (flow-based alternating inversion recovery) images of a flow phantom.We have also implemented magnetic resonance impedance tomography (MR-EIT) in phantoms at ULF. Knowing the electrical impedance of biological tissue is important for, e.g., forward models of the head for

MEG/electroencephalography source localization. We will present phase-maps showing the effects of the applied EIT currents in phantoms.

Poster 087

Using ULF MRI for Localization of Superparamagnetic Contrast Particles

Evgeny Burmistrov; Michelle A. Espy; Per Magnelind; Andrei Matlashov; Henrik Sandin; Petr Volegov; Los Alamos National

Laboratory, Los Alamos, NM There are many applications where the detection of small quantities of cells is important. An example is the early, specific detection of different kinds of cancer cells. The method relies on targeting of cells using antibody labeled single-core magnetic nanoparticles. Super-paramagnetic relaxometry is then used for detection of targeted cells with very high specificity; only bonded (immobilized) nanoparticles will be detected via NÉel relaxation. By combining this approach with ultra-low field magnetic resonance imaging using the same instrumentation, anatomical information can be combined. The same magnetic nanoparticles are used for T2-weighted MRI. The result will be the ability to detect and image clusters of about 1000 cells. It may provide a diagnostic tool for detecting cancer at very early stages.

DIFFUSION & FLOW, 088 - 099

Poster 088

Industrial Applications of DOSY NMR on Various Types of Synthetic Polymers

Chulsoon Moon; SK Innovaation Global Technology, Daejeon, South Korea

DOSY NMR was applied to study varous types of polyemrs for industrial purposes. In particular it was successfully used as a method to moniotr block copolymer polymrerization. In many cases synthetic polymers are made up of at least two different chemical species, having multiple distributions of various characteristics such as molecular weight and composition. Although the resulting 1H NMR spectrum does contain the signals expected for the block copolymer it is impossible to establish whether they belong to the polymer mixtures or to the corresponding block copolymers only by 1H NMR result. Here, we have demonstrated a potential of DOSY for the analysis of block copolymers distinguished from the polymer mixture as well as to account for the GPC-IR results.

Poster 089

3D BEST- DOSY, 3D COMPACT- IDOSY and 3D MQ- DOSY: New Tools for the Analysis of Complex Mixtures

Matsyendra Nath Shukla; Kavita Dorai; Department of Physics,IISER Mohali, Punjab, India

Diffusion-ordered spectroscopy (DOSY) is a powerful NMR experiment useful in separating signals from different components of a complex mixture. The 2D DOSY experiment has limited potential to differentiate between severely overlapped signals in a mixture. A number of 3D DOSY techniques have been developed to overcome this problem, wherein additional resolution is obtained by dispersing signals in the third dimension by appending a standard 2D pulse sequence to a DOSY experiment. Two new 3D diffusion-ordered heteronuclear (BEST-DOSY, COMPACT-IDOSY) and a homonuclear (3D MQ-DOSY) experiments have been



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designed and experimentally implemented on a mixture of amino acids, commercial gasoline and a mixture of flavonoids rutin and quercetin. Results of our recent studies are discussed.

Poster 090

Compressed Sensing for Motion and Flow: Dynamic Imaging and Propagator Measurements

Jeffrey Paulsen1; Sohyun Han2; Gang Zhu3; Youngkyu Song4; Gyunggoo Cho4; Yi-Qiao Song1; Hyungjoon Cho2; 1Schlumberger, Cambridge, MA; 2Nano-Bio Science and

Chemical Engineering, UNIST, Ulsan, Korea; 3Bruker Biospin, Billerica, MA; 4Korea Basic Science Institute, Ochang, Korea

Magnetic resonance techniques for flow and motion can almost always benefit from the encoding of additional dimensions and faster acquisitions. We examine the application of compressed sensing for the reconstruction of 1) multi-dimensional propagator measurements for the characterization of anisotropic structures and 2) dynamic contrast imaging (DCE) used to estimate tissue perfusion/permeability. Reducing the number of acquisition steps is the simplest way to acquire multi-dimensional propagator measurements in practical times, and to improve the compromise of frame rate and image resolution in DCE. We show that the application of compressed sensing is an effective way to reconstruct these experiments, where simple functional forms or sparse spectra found in spectroscopy are not available as priors.

Poster 091

A Possible Alternative towards Quantitative Diffusion NMR Data

Caroline Barrère; Pierre Thureau; André Thévand; Stéphane Viel; Aix-Marseille Univ. & CNRS, ICR UMR 7273, Marseille,

France Pulsed Gradient Spin Echo (PGSE) experiments constitute a powerful tool for analyzing mixtures because they can separate the NMR spectra of each component, but they are intrinsically non-quantitative due to the signal attenuation caused by longitudinal (T1) and transverse (T2) relaxation during the long pulse sequence delays. Alternatively to the quantitative Direct Exponential Curve Resolution Algorithm (qDECRA) approach proposed by Antalek, this work presents a strategy that renormalizes this relaxation attenuation using estimates of the T1 and T2 relaxation times for the nuclei in the mixture, as obtained with the pulse sequence used to record the PGSE experiment. It is shown that only three experiments need to be recorded, leading to higher quantification accuracy than qDECRA with less experimental time.

Poster 092

Pulse Field Gradient Diffusion NMR Characterizations of Perfluoro Quaternary Ammonium Ion Exchange

Membranes Yuan Yang; Colorado School of Mines, Golden, CO

Fuel Cells are a promising type of energy conversion device. Transport of ions and other chemical species through fuel cell membranes is important to understand its effectiveness and by extension membrane conductivity and morphology. Pulse gradient stimulated echo (PGSTE) nuclear magnetic resonance (NMR) spectroscopy was applied to characterize commercially produced sulfonyl ionomer with various

quaternary ammonium cations. Diffusion coefficients of species transport through the membranes were performed and correlated to membrane conductivities. Since transport of ions can also be related to morphology, we also investigated diffusion on different length scales and the restriction of diffusion in the membranes. Preliminary data has shown promising potential of perfluoro quaternary ammonium membranes as anion exchange membranes.

Poster 093

Studies of Aggregation of Organic Dyes as With NMR Christopher Lopez; student, Miami, FL

In this work, we present 1H-NMR studies of aggregation of the organic dyes, Sunset Yellow and Direct Blue. To characterize the aggregation, measurements of the diffusion rates, T1 and T2 relaxation times, and chemical shift changes as a function of concentration and temperature were performed and were used to analyze the aggregation dynamics. Finally, the predictions from different models of aggregation, such as the isodesmic model, were compared to our experimental results.

Poster 094

Simultaneous Measurements of Chronoamperometry and Low-Voltage Electrophoretic NMR for an Aqueous LiCl

Solution Kikuko Hayamizu1; Yuichi Aihara2; 1National Institute of

Advanced Industrial Science, Tsukuba, Japan; 2Samsung Yokohama Institute, Osaka, Japan

Electropherotic NMR (ENMR) measures ion migration of individual species in a bulk under an electric field. The chronoampetrometry (CA) observes a current profile under an electric potential. Electrochemically, however, it is difficult to observe individual ion transports in the bulk remote from the electrodes. In this study the simulteneous measurements of the ion movement at the electrodes and in the bulk were performed by connecting the CA measurement through a trigger generated by NMR pulse sequence. The electric field is applied on a NMR cell located in magnetic field. At the electrodes, the current decayed quickly by monitering with a potentiostat, and after the Li+ and H2O in the bulk started to migrate detecting by 7Li and 1H resonance.

Poster 095

Using Diffusion Ordered NMR Spectroscopy (DOSY) to Validate Ion-Mobility Mass Spectrometry (IMMS) Data Donald Stec; C. Ruth McNees; Janel McLean; Jody May;

John McLean; Brian Bachmann; Vanderbilt University, Nashville, TN

In this study, DOSY NMR experiments are being used to validate ion-mobility mass spectrometry bycorrelating gas-phase collision data with solution state diffusion measurements with the intention of potentially using IMMS to calculate gas phase diffusion coefficients for complex reaction mixtures where techniques like DOSY are ineffective due to peak overlap. Specifically, we have compared results for a series of natural products, short peptides of various lengths, and some common proteins. Initial results indicate a linear relationship exists between these measurements even after changing solution state parameters such as solvent viscosity and temperature. The goal of this study is to determine whether changes in the slope of the linear fits can be used relate IMMS data to their solution phase counterpart.



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Poster 096 Utilizing DOSY NMR Spectroscopy to Probe the Molecular

Size of Nano-particle Materials Abdul-Hamid Emwas; Muhammad Hussain; King Abdullah University of Science and Technology, Thuwal, Kingdom of

Saudi Arabia Nanoscale Ionic Materials (NIMs) are a new class of nanomaterials which consist of an inorganic nanoparticle core with oligomeric chains densely attached to the nanoparticle core. NIMs are unique among hybrids in that each of the components that make up the materials is itself nanoscale hybrids. We used a Two-Dimensional Diffusion-Ordered (DOSY) NMR Spectroscopy approach to compare the relative size of three NIMs compounds with different corona. In agreement with published report for similar system, our results show that the nanoparticle sizes were found to be between 2-5 nm. The results show that the DOSY approach is useful to compare the size of nanoparticles and it can differentiate between the sizes of different NIMs compounds.

Poster 097

NMR Diffusion Studies of Inverse Freezing in Mixtures of a-cyclodextrine and 4-methylopyridine

Piotr Garbacz1, 2; William Price2; 1University of Warsaw, Warsaw, Poland; 2University of Western Sydney, Penrith,

Australia Inverse freezing takes place when the heating of a system causes a reversible transition from the liquid to the crystalline solid state. This rare phenomenon can be observed in a mixture of a‑cyclodextrine (aCD) and 4‑methylopyridine (4MP). Below transition temperature (Tif) aCD:4MP mixture is a transparent liquid; above Tif it forms white crystals. The diffusion coefficients of aCD and 4MP were determined using 1H NMR diffusion measurements using a stimulated echo based sequence. At low temperatures, T < 280 K, the diffusion of aCD diffusion is non-Arrhenius but becomes Arrhenius in the range 280 K < T < 320 K. In contrast to aCD, the temperature dependence of the 4MP diffusion coefficient exhibits Arrhenius behaviour for all temperatures below Tif.

Poster 098

PASL-like Pseudo Random Amplitude Modulation: A Phantom Study

Xiaowei Zou1, 2; Truman R. Brown2; 1Columbia University, New York, NY; 2Medical University of South Carolina,

Charleston, SC It has been previously shown that Pseudo Random Amplitude Modulation (PRAM) [1,2,4] directly measures transit time distribution, providing a benefit to Arterial Spin Labeling (ASL) [3] techniques. Here we further investigate the PRAM properties in pulsed ASL using a parabolic flow phantom. Our results indicate that the while PASL-like PRAM can accurately measure flow velocities, it can generate complicated patterns associated with its modulation algorithm.

Poster 099

Pulse-Field-Gradient NMR Study of Hydrogen Bonding in EMIM Acetate-water Mixtures

Damodaran Krishnan Achary; University of Pittsburgh, Pittsburgh, PA

We demonstrate the application of PFG NMR spectroscopy to study the dynamics and hydrogen bonding of

water in the Ionic liquid [emim+][CH3COO-]. Ionic liquids generally have high CO2 solubility and are considered a very good medium for CO2 capture. [emim+][CH3COO-] is a potentially important ionic liquid for CO2 capture due to its high solubility and selectivity. It is, however, hydroscopic. Since flue gas mixtures contain moisture, it is important to understand the interaction of water with [emim+][CH3COO-]. It is known that the presence of water in ILs can increase or decrease CO2 solubility. To better understand the role of water in [emim+][CH3COO-], we have used PFG NMR spectroscopy.

DYNAMICS, 100 - 113

Poster 100

Glassy Dynamics of Non-solvent Related Modes near Protein Glass Transition Temperature Revealed by

Deuteron NMR Liliya Vugmeyster1; Dmitry Ostrovsky1; Gina Hoatson2;

Robert L. Vold2; 1University of Alaska Anchorage, Anchorage, AK; 2College of William and Mary, Williamsburg, VA

The dynamical glass transition of proteins is thought to be caused primarily by freezing of collective solvent-related modes of motions. We show direct site-specific evidence that non-solvent related modes play a part in this transition. We probe fast methyl group dynamics of several key methyl groups in chicken villin headpiece subdomain protein by deuteron solid-state NMR relaxation over a wide temperature range. At high temperatures, the hydrophobic core methyl groups exhibit essentially identical pico-second time scale dynamics with mono-exponential magnetization decays. The onset of glass-like behavior is manifested by non-exponentiality of the magnetization decay curves as well as non-Arrhenius temperature dependence of the relaxation rates below ~175K. This behavior is not dependent on the hydration state of the protein.

Poster 101

Exchange-Induced Relaxation in the Presence of a Fictitious Field

Dennis Sorce1; Timo Liimatainen2; Silvia Mangia1; Michael Garwood1; Shalom Michaeli1; 1CMRR, University of

Minnesota, Minneapolis , MN; 2Department of Biotechnology and Molecular Medicine, Kuopio, Finland

We have derived expressions for exchange-induced relaxation for two site fast exchange in the third rotating frame. The method of derivation is based on the density matrix formalism and is valid in the fast exchange regime. The methods proposed can be used for the description of exchange-induced relaxations in higher rotating frames of rank n > 2.

Poster 102

Electric Field NMR and Spin Relaxation in Propylene Carbonate

Yujie Qiu1; Wingchi Edmund Kwok2; Joseph Hornak1; 1RIT, Rochester, NY; 2University of Rochester, Rochester, NY

The effect of an electric field (E) on the 1H spin-lattice and spin-spin relaxation rates (R1and R2 respectively) was studied in a search for a dynamic functional MRI (fMRI) phantom. Our goal is to rapidly change the R2 of the polar liquid propylene carbonate by the application of E, thus mimicking the change in R2

* from the blood oxygen level dependent (BOLD)



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response used in fMRI. Electric fields can change the dipole-dipole interaction, anisotropic part of the scalar interaction, and chemical-shift anisotropy of spins in polar molecules, and hence R1 and R2. Though this change was too small, E also changed the echo modulation, causing an effective change in R2 which can be used to mimic the BOLD response.

Poster 103

Dynamics of 1-Butyl-3-methylimidazolium Trifluoromethanesulfonimide at Silica Surfaces

Kee Sung Han; Edward W. Hagaman; Oak Ridge National Laboratory, Oak Ridge, TN

The rotational and translational motion of the cation of the room-temperature ionic liquid (IL) 1-butyl-3-methylimidazolium trifluoromethanesufonylimide, [C4mim][Tf2N] were measured as a function of loading within the pores of meso-porous silica (KIT-6). Fractional filling of the pore volume, f=1~0.11, where f=1 represents the fully filled internal volume, were studied. 1H and 13C T1 and 1H pulsed-field gradient NMR (PFG-NMR) were used to obtain rotational correlation times, tc, and diffusion coefficient, D, respectively. At room temperature, D becomes smaller and approaches an asymptotic value of 10-11 m2s-1 as the theoretical coverage becomes less than a monolayer. The reduction in 1H T1 for the imidazolium ring of confined ILs suggests the existence of relatively strong interaction between the imidazolium ring and silica surfaces.

Poster 104

Dynamics of the Binding Surface of RRM Proteins Gregory DeKoster; Kathleen Hall; Washington University

School of Medicine, St. Louis, MO Human U1A and Drosophila SNF proteins are phylogenetically conserved RNA binding proteins. They consist of two RNA recognition motifs (RRMs) each with an α/β fold, but RNA binding occurs on the surface of the β sheet of RRM1 only. Thermodynamic coupling between beta-sheet residues Tyr-Gln-Phe suggest these residues form an interacting network to create the RNA binding site that also encompasses a proximal protein loop. Here, we measure the relaxation dispersion of backbone NH and side-chain NH2 in order to probe conformational exchange patterns within the network in wild type and YQF mutants of U1A and SNF RRMs to develop a dynamic physical model of their interactions.

Poster 105

Non-covalent Dimerization of Ubiquitin and Its Implication in the Structure of K63-linked Di-ubiquitin

Liu Zhu; Tang Chun; Wuhan Institute of Physics and Mathematics, Hubei, Wuhan, China

Multiple ubiquitins can be covalently linked via an isopeptide bond to form a di- and poly-ubiquitin. Depending on the site of the linkage, a di- and poly-ubiquitin may adopt a distinct quaternary structure, interacting with specific ubiquitin-binding domains (UBDs) in its partner proteins. Employing paramagnetic relaxation enhancement (PRE), a solution NMR technique that affords long-range distance information for lowly populated species, we have visualized the ensemble structure of the non-covalent ubiquitin dimer. Further, we detected the intermolecular interaction of K63-linked dimer ubiquitin, using a similar interface with non-covalent dimer ubiquitin. Covalent linkage restricts the rotation of two adjacent subunits, different from the freely rotating non-covalent ubiquitin dimer, while electrostatic repulsion

prevents inter-subunit contact between two covalently linked ubiquitins.

Poster 106

Improving the Accuracy and Quality of the NMR-based Globular Protein Structures – Implications for 15N

Relaxation Data Analysis Mariusz Jaremko; Institute of Biochemistry and Biophysics

PAS, Warsaw, Poland In comparison with X-ray structures the NMR-derived ones offer information on protein dynamics in solution, but suffer from lower accuracy and quality due to limited number of available experimental structural information. At present, there is a variety of protocols used for NMR-based protein structure refinement. In this study we examined currently available NMR-based structure refinement protocols using experimental data obtained for two different proteins: CsPinA and FCCH. Refinement of the NMR structure ensembles has been performed using CYANA, XPLOR-NIH, and XPLOR-NIH with explicit water refinement. Ensembles of refined CsPinA and FCCH proteins structures from previously published NMR data were analyzed (Procheck, ICING). Influence of the applied refinement protocol on the obtained dynamics parameters of CsPinA and FCCH proteins was discussed.

Poster 107

The Backbone Functional Dynamics of Cold-adapted peptidyl-prolyl Isomerase CsPinA - The 15N Relaxation

Studies at Four Magnetic Fields Lukasz Jaremko; University of Warsaw, Warsaw, Poland

The archeal CsPinA protein belongs to the class of the parvulin peptidyl-prolyl isomerases (PPIase) that regulate the protein mediated biological processes both at the stage of protein folding and within the native state. The CsPinA parvulin is a small enzyme that catalyzes the cis/trans isomerization of Xaa-Pro peptide bonds of target proteins at low temperature of 10oC. All parvulins of known so far 3D structures work at temperatures above RT and exhibit the same architecture of catalytic residues as the first archeal parvulin structure of CsPinA. Here we utilize the analysis of 15N relaxation data obtained at multiple magnetic fields and 10oC to investigate and better understand the cold-adaptation of psychrophilic parvulins.

Poster 108

Probing Protein Allostery in AAC(6')-Ii using a Multifaceted Biophysical Approach

Siqi Zhu; Lee Freiburger; Karine Auclair; Anthony K Mittermaier; McGill University Chemistry Department,

Montreal, Canada Aminoglycoside N-6’-acetyltransferase-Ii (AAC(6’)-Ii) is an antibiotic resistance causing enzyme that transfers an acetyl group from AcCoA to the 6’ position of aminoglycosides. This homo-dimeric enzyme has been shown to follow an ordered bi-bi mechanism with acetyl coenzyme A (AcCoA) binding first. We have previously developed a combined approach using isothermal titration calorimetry (ITC), nuclear magnetic resonance (NMR) and circular dicroism (CD) to explore the link between AcCoA binding thermodynamics, structural plasticity, and allostery at atomic resolution. Our current work



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focuses on using the same approach to study aminoglycoside binding as well as the formation of ternary complexes by introducing a second substrate. This presentation will summarize our preliminary results on binding behavior and its dependence on substrate and addition order.

Poster 109

Pulsed Field Gradient NMR and Molecular Dynamics Studies of Self-Diffusion in Unidimensional

Aluminosilicate Nanotubes Muslim Dvoyashkin1; Clifford R Bowers1; Ipek Yucelen2;

Sankar Nair2; Ji Zang2; David Sholl2; Aakanksha Katihar1; Sergey Vasenkov1; 1University of Florida, Gainesville, FL;

2Georgia Institute of Technology, Atlanta, GA Diffusion of tetraflouromethane in aluminosilicate nanotubes was studied by means of pulsed field gradient NMR (PFG) and molecular dynamics (MD) simulations. The application of a high magnetic field and high magnetic field gradients allowed 13C PFG NMR measurements of diffusion to be performed under conditions of sufficiently high signal-to-noise ratios for a broad range of tetraflouromethane loadings. Measured PFG NMR data were analyzed to obtain the diffusivities for one-dimensional diffusion of CF4 inside the nanotube aggregates where the sorbate displacements exceeded the average length of individual nanotubes. The experimental CF4 diffusivities inside the nanotube aggregates were then compared with those obtained by MD for diffusion inside the defect-free nanotubes.

Poster 110

Heterogeneity of Homopolymer and Heteropolymer Microgels by NMR

Andreea Cristina Balaceanu; Dan E. Demco; Andrij Pich; Functional and Interactive Polymers, Aachen, Germany

The Flory temperature-induced volume transition theory for microgels was extended to account for a crosslinker density distribution. We have characterized quantitatively homo (PVCL) and copolymer (PVCL:PNIPAAm/PNIPMAAm) microgel systems in the bimodal crosslink density heterogeneous approximation. High resolution 1H transverse magnetization relaxation NMR proved directly the existence of a bimodal heterogeneous morphology of the microgel particles. The ratio of the crosslink density in core and corona, evaluated from the T2 times of each decay components, was related to the Flory transition theory parameter, the number of subchains, through the scale invariant theory of polymer networks. By fitting the dynamic light scattering temperature transition data with the extended Flory transition theory state equation, we obtain quantitative information about the microgel particle.

Poster 111

Quantitative Comparison of Errors in 15N Transverse Relaxation Rates Measured using Two Different CPMG

Phasing Schemes Rieko Ishima; Wazo Z. Myint; University of Pittsburgh,

Pittsburgh, PA To elucidate the impact of the known phase alternation method on the accuracy of Carr-Purcell-Meiboom-Gill (CPMG) transverse relaxation experiment, we performed simulation and experiments of CPMG for 15N nuclei with and without the phase alternation. Our simulations show that R2 can be obtained accurately for a relatively wide spectral width, either

using the conventional phase cycle or using phase alternation when the r.f. pulse power is accurately calibrated. However, when the r.f. pulse is miscalibrated, the conventional CPMG experiment exhibits more significant uncertainties in R2 caused by the off-resonance effect than does the phase alternation experiment. Our experiments show that this effect becomes manifest under the circumstance that the systematic error exceeds that arising from experimental noise.

Poster 112

Ensemble Characterization of RNA Dynamics using NMR and MD simulations

Loic Salmon; Shan Yang; Hashim Al-Hashimi; University of Michigan, Ann Arbor, MI

Biologically important conformational changes of RNA remain extremely challenging to characterize due to the important coupling between local dynamics and large domain motions. The presented approach aims to combine interesting conformational sampling of molecular dynamics trajectories and the exquisite NMR RDC sensitivity to molecular motion to generate meaningful ensemble representative of the biophysical properties of HIV-TAR RNA. This approach is based on a Sample And Select procedure where the starting conformational pool is generated using MD simulations and thereafter, sub-ensemble selection is achieved using RDCs measured in different elongated or non-elongated constructions. By accommodating any level of elongation this approach will open a new avenue for quantitative analysis of RDCs measured under several different conditions of alignment.

Poster 113

The Loschmidt Echo as a Robust Decoherence Quantifier for Many-body Systems

Pablo R. Zangara1, 2; Axel D. Dente1, 2; Patricia R. Levstein1, 2; Horacio M. Pastawski1, 2; 1Instituto de Física Enrique Gaviola

(CONICET), Córdoba, Argentina; 2FAMAF (Universidad Nacional de Córdoba), Córdoba, Argentina

High efficiency many-body dynamics of spin systems using the Graphical Processing Unit enables us to study decoherence in many-spin systems. We numerically evaluate the Loschmidt Echo, which in NMR is the signal recovered after the time-reversal of a many-spin evolution. In particular, we consider two spin chains with planar Hamiltonians, which are weakly coupled by a general spin-spin interaction, including Ising (ZZ) and planar (XY) terms. Only the Hamiltonian in one of the chains is inverted, and thus the Loschmidt Echo smoothly degrades. Several regimes are identified, and particularly we analyze the exponential one described by the Fermi Golden Rule. Accordingly, decoherence rates are obtained and analyzed separately for each physical process present in the inter-chain interaction.

EDUCATION/FACILITIES, 114 - 115

Poster 114

Advanced Magnetic Resonance Capabilities at the Environmental Molecular Sciences Laboratory (EMSL) to

Accelerate Studies of Materials, Interfaces, and Biosystems

Nancy Washton; Sarah Burton; Michael Froehlke; David W Hoyt; Jian Zhi Hu; Nancy Isern; Don Rommereim; Andrew S.

Lipton; Paul Majors; Hardeep Mehta; Jesse Sears; Flaviu



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Turcu; Eric Walter; Karl Mueller; Pacific Northwest National Laboratory, Richland, WA

The Environmental Molecular Sciences Laboratory (EMSL) is a Department of Energy national scientific user facility, located at Pacific Northwest National Laboratory. The EMSL user facility houses magnetic resonance systems for applications such as 1) ultra high-field NMR for solid-state experiments at 900, 850, 800, and 750 MHz; 2) pulsed EPR spectrometers including a high-power, high-field (95 GHz) system; 3) an ultra high-field radiological wide bore NMR with capabilities for imaging, solution, and solid-state NMR including multi-receiver spectroscopy; and 4) a 500 MHz micro-imaging spectrometer for in-vivo magnetic resonance imaging, localized NMR spectroscopy, and NMR diffusion studies. Capabilities and expertise that contribute to a problem-solving research environment in areas including materials development, catalysis, geosciences, structural biology and metabolomics will be highlighted.

Poster 115

Resource for NMR Molecular Imaging of Proteins Christopher V. Grant; Chin H. Wu; Stanley J. Opella;

University of California San Diego, La Jolla, CA The developments of methods and instrumentation, and their application to membrane bound proteins will be presented. The Resource is dedicated to solid-state NMR spectroscopy for the study of protein structure and function. Recent solid-state NMR methods, applications and developments will be summarized, including solid-state NMR probes optimized for magic angle spinning and static oriented methods. The Resource for NMR Molecular Imaging of Proteins is supported by the National Institute of Biomedical Imaging and Bioengineering (P41EB002031).

EXOTICA & BEYOND, 116 - 126

Poster 116

Monitoring in situ Copper Electrodeposition Reaction Using NMR Unilateral

Luis Fernando Cabeça; Luiza Maria da Silva Nunes; Luiz Alberto Colnago; EMBRAPA Instrumentation, São Carlos,

Brazil We are showing by the first time the coupling of electrochemistry and NMR Unilateral (UNMR) spectrometer (constructed in a classical “U-shaped” geometry). The measurements provide better conditions because the electrochemical reaction takes place outside of the radio frequency (RF) coil probe. The work evaluated the potential of combination between UNMR and electrochemical to monitor in situ cooper electrodeposition. The Cu+2 concentrations during the reaction were calculated using CPMG decay (every ten minutes during 3 hours). As expected the Cu+2 concentration decrease rapidly with the electrodeposition until approximately 130 min, and then remained constant. After 3 hours reaction, 57.5% of ions in solutions were deposited on the work electrode. These results bring good prospects for monitoring electrochemical reactions in situ.

Poster 117

100x Enhancement of Hyperpolarized Xenon-129 Dissolved-phase Signal During Functional MR Studies of

Fatty Tissues

Rosa Tamara Branca1, 2; Arjun Khanna2; Matthew Freeman3; 1Department of Physics and Astronomy, University of, Chapel Hill, NC; 2Chemistry Department, Duke University, Durham,

NC; 3Department of Medical Physics, Duke University, Durham, NC

Due to its high solubility in blood and tissue and its high sensitivity to the local environment, HP 129-Xe has long been considered a unique probe for imaging living tissues. Unfortunately, imaging results have been disappointing mainly because of the low concentration of xenon that dissolves in tissue. Here we report the first HP 129-Xe functional MR studies of fatty tissues, specifically Brown Adipose Tissue (BAT). Our studies show that HP-129Xe is highly sensitive to BAT activity during which more than a 100x enhancement of the HP 129-Xe dissolved-phase signal can been observed.

Poster 118

A Dynamical Theory of Spin Relaxation Timothy R. Field; Alex D. Bain; McMaster University,

Hamilton, Canada The dynamics of a spin system is usually calculated using the density matrix. However, the usual formulation in terms of the density matrix predicts that the signal will decay to zero, and does not address the issue of individual spin dynamics. Using stochastic calculus we develop a dynamical theory of spin relaxation whose origins lie in the component spin fluctuations. This entails consideration of random pure states for individual protons, and how these pure states are correctly combined when the density matrix is formulated. Both the lattice and the spins are treated quantum mechanically. Such treatment incorporates both the processes of spin-spin and (finite temperature) spin-lattice relaxation. Our results reveal the intimate connections between spin noise and conventional spin relaxation.

Poster 119

Below Cut-off Traveling Wave NMR at 16.4T: Interference of Propagating Modes in a High Dielectric-filled

Waveguide Alexey Tonyushkin1; Gregor Adriany2; Dinesh Deelchand2;

Michael Garwood2; Andrew Kiruluta1; 1MGH, Harvard Medical School, Boston, MA; 2University of Minnesota Medical School,

Minneapolis, MN At ultra-high field strength, the propagation wave vector of the excitation field can no longer be ignored as the wavelength becomes comparable to the imaging volume, particularly if the medium dielectric constant is large. Here, we present our latest developments on a traveling wave waveguide system allowing mode propagation in a 16.4 T horizontal bore NMR imaging system. The waveguide consists of a metal bore of the magnet and an acrylic tube filled with high dielectric material. The excitation of a waveguide is achieved through a transmit-receive loop coil probe placed at one or both ends of the guide. We describe propagating mode phenomena that were observed in the dielectric and discuss the implications for ultra-high field NMR.

Poster 120

Time Domain NMR Spectroelectrochemistry: Monitoring in situ Copper Electrodeposition Reaction



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Luis Fernando Cabeça; Luiza Maria da Silva Nunes; Paulo Falco Cobra; Luiz Alberto Colnago; EMBRAPA

Instrumentation, São Carlos, Brazil The combination of electrochemical (EC) and Nuclear Magnetic Resonance (NMR) has been rarely performed due to distortion of the static magnetic field (B0) homogeneity. Because of the bench top NMR (Time Domain – TDNMR) low homogeneity, the distortion caused in magnetic field by the electrodes is not critical. Therefore, the copper electrodeposition reaction can be monitored using the Carr-Purcel-Meiboom-Gill (CPMG) to measure transverse relaxation time. The results showed that Cu+2 concentration decreased rapidly with the electrodeposition until 100 min, and then, remained constant. After 3 hours reaction the Cu+2

concentration was 2x10-3 M, corresponding to 10% of the initial Cu+2 concentration. The measures show that EC-TDNMR combination can be very fast, simple and an efficient technique to monitor electrodeposition reaction.

Poster 121

Multiple Spin Coherences and the Time Evolution of a Magic Echo

Steven Morgan1; Vadim Oganesyan2; Gregory Boutis1; 1Brooklyn College/CUNY, Brooklyn, NY; 2College of Staten

Island/CUNY, Staten Island, NY We report on an average Hamiltonian treatment of a magic echo to second order. The degradation of time-reversal with increasing evolution time is shown theoretically and via simulation and experiment to be strongly influenced by finite pulse width effects. We investigate the spin dynamics under a magic echo sequence beyond the single-spin, single-quantum portion of the density matrix. In a sample of adamantane we observe that the evolution of multiple spin correlations following a magic echo is similar to the FID even though the overall signal amplitude decreased more than 50% for the longest magic echo measured. Additionally, the long-time portion of the coherences detected is observed to decay at the same rate for both the FID and magic echoes.

Poster 122

Methodology to Measure Temperature and Thermal Diffusivity in Intact Seeds and Seeds Inside Soils by

Time Domain NMR Maria Gabriela Aparecida Carosio1; Luiz Alberto Colnago2;

1Institute of Chemistry of São Carlos, São Carlos, Brazil; 2EMBRAPA Instrumentation, São Carlos, Brazil

Soil temperature is important in agriculture and affects directly the seed germination. Some seeds may survive in high temperature environment for days, but the seedling may die in few hours. Several NMR parameters are affected by temperature and can be used to monitor it. We are showing that we can use time domain NMR to measure temperature using oilseeds as a sensor. The measurement is based on the T2 dependence of oil viscosity and temperature. Although soil type doesn’t influence directly on the signal acquisition, it’ll be indirectly influenced, because the seed will heat more or less depending on the soil type. This study shows it is possible to obtain information in vivo and quickly, compared with other techniques.

Poster 123 The Chemical and Structural Characterization of Soil: A

Comprehensive Multiphase NMR Approach

Hussain Masoom1; Denis Courtier-Murias1; Ronald Soong1; Hashim Farooq1; Werner E. Maas2; Michael Fey2; Brian Andrew2; Jochem Struppe2; Howard Hutchins2; Sridevi

Krishnamurthy2; Rajeev Kumar3; Martine Monette3; Henry J. Stronks3; Alan Hume3; Andre J Simpson1; 1University of

Toronto, Scarborough, Canada; 2Bruker Biospin, Billerica, MA; 3Bruker Biospin Canada, Milton, ON

Comprehensive multiphase (CMP)-NMR is useful to investigate complex environmental samples because it has the capability to study solid, liquid, and gel-phase (HR-MAS) components without sample pre-treatment. Here we have used CMP-NMR to look at the structure and chemistry of soil colloids at the water interface in whole untreated samples. 13C CP-MAS experiments on a wet and dry soil indicate that carbohydrate and aliphatic moieties are present on the surface of soils while aromatic and proteinaceous components lay buried in the solid phase and have been confirmed by 1H experiments. Additionally, more penetrating solvents and multidimensional NMR were used to characterize the various soil components, strengthening the notion that soil organic matter is made of small subunits which form supra-molecular associations.

Poster 124

Diamond Magnetometer near the Shot Noise Limit at Room Temperature

Chang Shin1, 2; Claudia Avalos1, 2; Mark Butler1, 2; David Trease1, 2; Scott Seltzer1, 2; Daniel Kennedy1, 2; J. Peter

Mustonen1, 2; Victor Acosta3, 4; Dmitry Budker3, 4; Alexander Pines1, 2; Vikram Bajaj1, 2; 1Department of Chemistry,

University of California, Berkeley, CA; 2Materials Science Division, LBNL, Berkeley, CA; 3Department of Physics, University of California, Berkeley, CA; 4Nuclear Science

Division, LBNL, Berkeley, CA The negatively charged nitrogen vacancy centers (NV–), substitutional point defects in diamond have recently been exploited in several applications including magnetometry. We operate a nitrogen vacancy (NV–) diamond magnetometer at ambient temperatures and study the dependence of its bandwidth on experimental parameters including optical and microwave excitation powers. We introduce an analytical theory that yields an explicit formula for the response of an ensemble of NV– spins to an oscillating magnetic field, such as in NMR applications. We measure a detection bandwidth of 1.6 MHz and a sensitivity of 4.6 nT/√Hz, unprecedented in a detector with this active volume and close to the photon shot noise limit of our experiment.

Poster 125

NMR of Polyoxometallates (POM): Mo132 Meets Amino-Acids

Erhard T.K. Haupt; Department Chemistry University Hamburg, Hamburg, Germany

Previous studies concerning the lipophilic attraction of a ball-like polyoxometallate like Mo132 loaded with aliphatic chain internal linkers (like actetates) towards molecules with intermediate aliphatic chains like hexane, hexanol….[Chem. Eur. J. 17, 9634 (2011)] are extended to more biological interesting compounds like simple amino-acids. The surprising result is, that the amino-acids interact clearly with the Mo132-molecule, but there is no contact with the internal part of the moiety. Careful NMR-studies show (CSM and DOSY) that there is a contact, but in form of a slow exchange of the



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amino-acids on top of the pores with the free amino-acid in solution. Various molecules support this result. This opens the way to POM-structures covered with biologically active compounds.

Poster 126

Experimental Demonstration of Long-lived Singlet States between Chemically Equivalent Spins

Yesu Feng; Duke University, Durham, NC “Hyperpolarization” methods for carbon and nitrogen have dramatically increased the bulk magnetization for many different biologically relevant molecules. However, in vivo applications are restricted to very few molecules due to the short T1 relaxation time of most molecules. Here we present a pulse sequence strategy to extend signal lifetime by storing the bulk magnetization as population differences between the singlet and triplet states. We use diethyl oxalate-13C2 to demonstrate the efficacy of the pulse sequence; both simulations and experimental results are presented.

HYPERPOLARIZATION & NEW DETECTION METHODS,

127 - 163

Poster 127 Novel Polarizing Agents for High-Field Dynamic Nuclear

Polarization Bjorn Corzilius1; Albert Smith1; Olesya Haze1; Matthew Kiesewetter1; Claudio Luchinat2; Ivano Bertini2; Timothy Swager1; Robert Griffin1; 1MIT, Cambridge, MA; 2CERM,

Florence, Italy We present new advances on the development of organic mono- and biradicals. We introduce two polarizing agents soluble in typical glycerol/water cryoprotecting matrix. A highly water-soluble BDPA derivative exceeds enhancements obtained with trityl and will be interesting for EPR. We also developed a water-soluble rigid biradical for cross effect DNP that outperforms TOTAPOL. We discuss impact of structure, solubility and electronic coupling on DNP performance. We also present recent results on high-spin metal (MnII, GdIII) complexes as polarizing agents for solid effect (SE) DNP. We have shown earlier that significant 1H enhancements can be obtained under MAS conditions at 5 T. The narrow EPR linewidth also allows efficient direct polarization of 13C by SE not feasible with conventional polarizing agents.

Poster 128

Dynamic Nuclear Polarization of 107,109Ag Complexes Lloyd Lumata; Matthew E Merritt; Zohreh Hashami; S. James Ratnakar; Zoltan Kovacs; University of Texas Southwestern

Medical Center, Dallas, TX Silver complexes are important because the Ag+ ion has an extensive organic, inorganic, and medicinal chemistry. For instance, the diphosphine complexes [Ag(dppp) 2]+ and [Ag(dppe) 2]+ have shown potent anticancer properties and [Ag(dotete)] + was suggested for targeted radiotherapy of cancer. Ag NMR is a useful method for the structural characterization of silver complexes, however it is hindered by low sensitivity due to the low γ of the Ag nuclei. Here we show that both isotopes of silver (107Ag and 109Ag) can be simultaneously polarized by dynamic nuclear polarization (DNP), thus allowing NMR characterization of Ag complexes in the millimolar concentration range. Since both isotopes

have long relaxation times T1, the hyperpolarized NMR signal of both isotopes can be detected consecutively.

Poster 129

Investigation of Protein Folding using Dynamic Nuclear Polarization Enhanced NMR

Mukundan Ragavan; Hsueh-Ying Chen; Giridhar Sekar; Christian Hilty; Texas A&M University, College Station, TX

Biomolecular NMR is typically employed to study steady-state processes because of the lack of sensitivity. Solid-to-liquid state dynamic nuclear polarization (DNP) provides large signal enhancements and enables monitoring of transient processes without the need for signal averaging. While this technique has in the past been used to study enzyme catalyzed reactions, here, we extend its applicability to study the dynamic process of protein folding in real time. Employing pH jump followed by measurement of time resolved NMR spectra, the folding of a ribosomal protein, L23, was observed. The folded and unfolded populations, obtained using decomposition of the DNP spectra with respect to reference spectra, were then fitted to a kinetic model which yields the folding rate constant.

Poster 130

Exploring Crystalline Self-Assembled Bis-Urea Macrocycles and L-Phenylalanine Dipeptide Nanotube

Cavities by Hyperpolarized Xenon-129 NMR Muslim Dvoyashkin1; Chris Akel1; Linda S Shimizu2; Sergey

Vasenkov1; Clifford R Bowers1; 1University of Florida, Gainesville, FL; 2University of South Carolina, Columbia, SC

Hollow nanotubular structures have a wide range of applications in biology, chemistry, physics, and materials science. Elegant examples of self-assembled structures formed purely by hydrogen bonding include bis-urea macrocycles and various dipeptides. A key advantage of the use of rigid macrocycles based on urea-urea hydrogen bonding is the ability to tune the size and shape of the cavities for specific purposes. The supramolecular aggregation of the dipeptide L-phenylalanyl-L-phenylalanine is important due to its potential role in the formation of amyloid fibers by Alzheimer’s b-amyloid polypeptide, where -F19-F20- is a key structural motif. We explore the geometry and filling of the intrachannel void spaces in the two different crystalline self-assembled hydrogen bonded molecular nanotube materials using continuous-flow hyperpolarized xenon-129 NMR spectroscopy.

Poster 131

Solid-to-liquid State DNP of Large Molecules Christian Hilty; Sean Bowen; Hsueh-Ying Chen; Youngbok Lee; Mukundan Ragavan; Giridhar Sekar; Haifeng Zeng;

Texas A&M University, College Station, TX Solid-to-liquid state dynamic nuclear polarization (DNP) is a popular hyperpolarization technique for enhancing NMR signals in the liquid state by several orders of magnitude. Up to present, solid-to-liquid state DNP has been applied primarily in conjunction with small molecules, due to challenges including sample dissolution and spin relaxation prior to the acquisition of an NMR spectrum. Here, we present several strategies for polarization of macromolecules. Polarization from a hyperpolarized ligand can be transferred to a protein, where resonances from the vicinity of the binding site are enhanced. Isotopically labeled proteins are amenable



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to direct DNP polarization, enabling applications such as the determination of intermolecular interactions or protein folding. Finally, polymerization reactions can be studied by in-situ incorporation of hyperpolarized monomers.

Poster 132

High-Field 29Si, 13C and 27Al Dynamic Nuclear Polarization of Nanostructured Inorganic Materials

Olivier Lafon1; Fabien Aussenac2; Melanie M Rosay3; Aany Sofia Lilly Thankamony1; Xingyu Lu1; Julien Trebosc1; Herve

Vezin1; Jean Paul Amoureux1; 1University of Lille Nord de France, Villeneuve D'ascq Cedex, France; 2Bruker Biospin,

Wissembourg, France; 3Bruker BioSpin Corporation, Billerica, MA

The extension of high-field MAS DNP to inorganic materials faces the issue of polarization distribution throughout non-protonated solids, in which 1H-1H spin diffusion is precluded. We show here how direct 29Si DNP allows circumventing this limitation in the case of siliceous materials with applications in photonics, nanotechnology and catalysis. Signal enhancement of up to 30 were measured by direct 29Si DNP. Furthermore, direct and indirect 29Si DNP via 1H are complementary. The former enhances both the surface and subsurface 29Si signals, while the latter enhances the surface 29Si signals selectively. Furthermore, other recent applications of high field DNP for meso- and micro-porous solids as well as nanoparticles will be presented.

Poster 133

Low Temperature DNP for Characterization of Static Samples using 2D-exchange Experiments

Alexey Potapov; Kent Thurber; Wai-Ming Yau; Robert Tycko; National Inst of Diabetes and Digestive and K, Bethesda, MD

A typical DNP experiment is carried out under MAS conditions at temperatures of ~80 K and require MW irradiation of significant strength. Alternatively, substantial DNP-enhancements can be obtained using lower power at lower temperatures. Here we demonstrate feasibility of DNP-assisted 2D-exchange experiments for characterization of amyloid fibrils and systematically study the optimal conditions for it. We constructed a 2-channel low-temperature NMR probe capable to withstand high-power decoupling periods. The experiments at 8 and 16 K have revealed a significant T2 relaxation of 13C. Optimization of polarizing agent concentration showed that triradicals DOTOPA-TEMPO show a remarkably fast magnetization build-up rates. The 2D-exchange experiment correlating the CSA’s of neighboring C’ nuclei in the Ab fibrils required only 4 hours of data collection.

Poster 134

Imaging Hydrophobic Interactions using Hyperpolarized 13C MR Spectroscopy at 14T

Kayvan Keshari; Mark Van Criekinge; John Kurhanewicz; David Wilson; UCSF, San Francisco, CA

A cyclodextrin model system was used to image hydrophobic interactions at 14T, using hyperpolarized (HP) 13C MR spectroscopy. [1-13C] benzoic acid (BA) was polarized via a dynamic nuclear polarization (DNP) approach and combined with varying concentrations of cyclodextrin in solution. A 3D frequency-selective imaging sequence was used to image the solutions, demonstrating variable loss of signal depending on the concentration of the cyclodextrin host. In a separate set of

studies, T1 experiments were performed on HP [1-13C] benzoic acid- cyclodextrin solutions were used to calculate KD, found to be similar to that previously reported. These results suggest that HP 13C spectroscopy could be employed in vivo to image ligand host interactions by T1 shortening.

Poster 135

Hyperpolarized 89Y-Texaphyrin as an NMR Sensor for Lactate

Lloyd Lumata1; Christian Preihs2; S. James Ratnakar1; Jonathan L Sessler2; Matthew E Merritt1; Craig R Malloy1; A.

Dean Sherry1, 3; Zoltan Kovacs1; 1University of Texas Southwestern Medical Center, Dallas, TX; 2University of

Texas at Austin, Austin, TX; 3University of Texas at Dallas, Richardson, TX

The lanthanide complexes of texaphyrins (pentaaza-expanded porphyrins) have attracted considerable interest because of a variety of biomedical applications. For instance, Gd(III)-texaphyrins have been proposed as MRI contrast agents due to their ability to selectively accumulate in tumors. Yttrium-89 is an attractive nucleus for the design of responsive NMR probes because of the sensitivity of the 89Y NMR chemical shift to the coordination environment of the Y(III) ion. However, direct detection of 89Y is difficult due to the low gyromagnetic ratio of 89Y. Here we show that the 89Y NMR signal of Y-texaphyrin can be enhanced several-thousand-fold using fast dissolution dynamic nuclear polarization (DNP) and that the 89Y chemical shift of Y-texaphyrin can be used to detect metabolites such as lactate.

Poster 136

Frequency Modulated Dynamic Nuclear Polarization Yonatan Hovav; Weizmann institute of science, Rehovot,

Israel During DNP the NMR signal is increased via microwave (MW) irradiation close to the EPR transitions of radicals which are added to the sample. While in most cases DNP is performed using continuous wave irradiation, it was recently demonstrated by Tycko and coworkers that field modulation can result in a further gain in signal. In this work show that modulation of the MW frequency can also be used to increase the DNP effect. We present a systematic study of nuclear enhancement as a function of the modulation amplitude and frequency, with the measurements performed using the 4-hydroxy TEMPO radical at low temperatures. Maximal enhancement was reached for fast oscillations.

Poster 137

Extension of the Singlet State Lifetime of N2O via Alteration of Temperature and Viscosity of

Dissolving Solvent Rajat Ghosh; University of Pennsylvania, Dept. of Radiology,

Philadelphia, PA Dipolar relaxation often limits polarization lifetime and the development of hyperpolarized magnetic tracers. Recently, it has been demonstrated that transferring spin order to a singlet state significantly increases the polarization lifetimes in systems where nitrous oxide is dissolved in a liquid solvent and that the longitudinal relaxation of nitrous oxide is largely dominated by the spin-rotation interaction. This finding indicates that unique strategies can further lengthen the singlet lifetime by altering the dissolving solvent’s



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characteristics. We investigate the effect of altering the temperature of the solvent and varying viscosity on the singlet state’s lifetime as well as the longitudinal polarization lifetime. We discuss strategies for extending the singlet lifetime of dissolved nitrous oxide by altering the properties of the solvent.

Poster 138

Precision Measurements and Calculations of Nuclear Spin Optical Rotation in Organic Liquids

Junhui Shi1; Suvi Ikäläinen2; Juha Vaara2; Michael V Romalis1; 1Princeton University, Princeton, NJ; 2University of

Oulu, Finland Nuclear spin optical rotation (NSOR) is a recently developed technique for detection of nuclear magnetic resonance (NMR) via rotation of light polarization. NSOR signals can reveal information about the nuclear chemical environment, but they are generally quite weak, especially for light nuclei. We perform precision measurements of NSOR in a range of organic liquids at 405 nm using a multi-pass optical cell to increase the rotation signal. We find that 1H NSOR can be used to distinguish between organic compounds and does not scale with either the Verdet constant or the inductive NMR signal. In addition, the recently developed techniques for first principles calculation of the NSOR gives results in good agreement with our measurements.

Poster 139

Retaining Polarization by Exploiting Slower T1 Relaxation of Hyperpolarized Spins at Low Field in Solution

Mark Van Criekinge; Kayvan Keshari; David M. Wilson; Daniel B Vigneron; John Kurhanewicz; UCSF - Radiology,

San Francisco, CA The dramatic increase in T1 relaxation rate of hyperpolarized spins (i.e. carbonyl carbons) at low magnetic field strengths is utilized to preserve more of the unrecoverable polarization of dissolved DNP samples. For in vivo studies, the field dependency of [1-13C] pyruvate is investigated to possibly allow the hyperpolarized spins to evolve inside of an animal at low field and then be transported to the magnet a later time to observe slower enzyme kinetics.

Poster 140

Hyperpolarization of 13C-phospholactate by PASADENA Roman Shchepin; Aaron Coffey; Kevin Waddell; Eduard Chekmenev; Vanderbilt University Institute of Imaging

Science, Nashville, TN We demonstrate that sodium 1-13C-phosphoenolpyruvate becomes hyperpolarized sodium 1-13C –phospholactate with 13C T1 = 36 s after molecular hydrogenation by PASADENA (Parahydrogen and Synthesis Allows Dramatically Enhanced Nuclear Alignment). This proof-of-principle study was conducted with a fully protonated molecular precursor. 13C was polarized to a level of 1 %, corresponding to nearly 4,000 fold sensitivity enhancement at 3 T. The relevant homo- and heteronuclear spin-spin couplings are reported. It is anticipated that deuterated 1-13C-phophoenolpyruvate will provide higher polarization.

Poster 141

Solvent-Free Dynamic Nuclear Polarization of Amorphous and Crystalline Ortho-terphenyl

Ta-Chung Ong1; Melody L. Mak-Jurkauskas3, 4; Joseph J. Walish2, 5; Vladimir K. Michaelis1; Andrew M. Clausen3, 4; Janet C. Cheetham3, 4; Timothy M. Swager2; Robert G.

Griffin1; 1Francis Bitter Magnet Lab, MIT, Cambridge, MA; 2Massachusetts Institute of Technology, Cambridge, MA;

3Amgen Inc., Cambridge, MA; 4Amgen Inc., Thousand Oaks, CA; 5DyNuPol, Inc., Cambridge, MA

Solid-state NMR is used extensively in the characterization of active pharmaceutical ingredients (APIs) in solid formulations. Signal enhancement by Dynamic Nuclear Polarization (DNP) offers a possibility to efficiently analyze pharmaceuticals. To accomplish this, understanding of the DNP process in a solvent-free matrix for amorphous and crystalline solids is required. Here we present a comparison of signal enhancements employing DNP for the glass-former ortho-terphenyl (OTP) in its amorphous/glassy and crystalline states. We observed 2-6 times stronger signal enhancement for the glassy OTP. This result motivates further studies to improve sample preparation methods and to design new molecules as radical source for DNP. Our aim is to improve polarization in crystalline samples and effectively implement DNP to solid-state NMR of drug formulations.

Poster 142

Opportunities for Solid State Dynamic Nuclear Polarization below 20 K

Ting Ann Siaw1; Shamon Walker1; Songi Han1, 2; 1Department of Chemical Engineering, UCSB, Santa Barbara,

CA; 2Department of Chemistry and Biochemistry, UCSB, Santa Barbara, CA

At high fields and low temperatures (below 20 K), dynamic nuclear polarization (DNP) can drastically enhance sensitivity while simultaneously provide unique physical insight into electron-nuclear correlations. At these temperatures, low power (< 90 mW) diode microwave sources already achieve high nuclear polarization, as we demonstrate with 61 % 1H polarization in a glycerol-water glass. Diode microwave sources offer the advantage of a large frequency tuning range (193-201 GHz for our system), which facilitates the acquisition of DNP frequency profiles. The versatility of our instrument allows us to extend DNP to study materials with intrinsic paramagnetic defects, e.g. hydrogenated amorphous silicon (a-Si:H). Here, DNP offers to elucidate the local nuclear structure around the paramagnetic defects through 1H, 29Si or 19F nuclei.

Poster 143

Hyperpolarized Xenon Chemical Shift Inversion Transfer (Hyper-CEIT)

Qing Luo; Haidong Li; Zhao Li; Qianni Guo; Shizhen Chen; Chaohui Ye; Xin Zhou; Wuhan Center for Magnetic

Resonance, Wuhan, China An indirect detection MRI method, named Hyperpolarized Xenon Chemical Shift Inversion Transfer (Hyper-CEIT), is presented here based on the similar signal enhancement strategy to CEST, but with an improved spin control manner. In comparison to the established methods, our new method achieves not only a higher contrast but also a lower duty cycle of pulses, which would be significantly important to in vivo MRI, especially human MRI with large size coils.



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Poster 144 Dynamic Nuclear Polarization NMR of Oxygen-17 using

Mono- and Bi-radical Polarizing Agents Vladimir K. Michaelis1; Evgeny Markhasin1; Eugenio Daviso1,

2; Bjorn Corzilius1; Albert Smith1; Judith Herzfeld2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge,

MA; 2Brandeis University, Waltham, MA Oxygen is the most abundant element on earth, and is involved in a variety of systems ranging from biological function to earth sciences. It is however a difficult molecule to study by NMR spectroscopy due to its inherent physical properties. 17O (I=5/2) suffers from low natural abundance (0.038%), moderately large quadrupolar couplings (~4 to 10 MHz) and a small gyromagnetic ratio (~1/8 of 1H). Our focus is on the oxygen environment within water of a glycerol/water glass. Results will be presented on a 212 MHz / 140 GHz DNP NMR spectrometer using both direct (17O) and indirect (1H) polarization via the cross-effect mechanism. Enhancements >100-fold have been recorded enabling us to perform 1D and 2D type experiments within hours.

Poster 145

13C Sub-second Metabolic MRI of Cancer using Parahydrogen Induced Polarization (PHIP)

Milton Truong1; Aaron Coffey1, 2; Roman Shchepin1; Kevin Waddell1; Eduard Chekmenev1, 2; 1Vanderbilt University Institute of Imaging Science, Nashville, TN; 2Vanderbilt

University, Nashville, TN 13C and 15N hyperpolarized metabolic contrast agents create opportunities to characterize and develop relationships between in vivo metabolic levels and cancer for early cancer detection and monitoring response to treatment. Here, hyperpolarized tracers are generated by molecular addition of parahydrogen gas to unsaturated molecular precursors using water soluble rhodium based molecular catalyst in a high-pressure chemical reactor, within a 48 mT magnet. Initial direct 13C MRI images of hyperpolarized tracers, using a balanced fast field echo (BFFE) sequence are shown to demonstrate the resolution obtainable with hyperpolarized tracers. The development of an enhanced 3D BFFE sequence with more sensitive indirect 1H detection and chemical selectivity potentially allows for improved spatial resolution and would enable imaging cancer metabolism in vivo.

Poster 146

The Inter-Connectivity of Multiple Adsorption Sites within MIL-53 (Al) Examined by 129Xe 2D EXSY NMR

Spectroscopy Caroline D. Keenan; Ernst Rößler; Juergen Senker; University

of Bayreuth, Bayreuth, GERMANY Here, we use hyper-polarized 129Xe 2D EXSY NMR to investigate the inter-connectivity of co-existing adsorption sites within MIL-53(Al) during the “breathing” phenomenon observed within this framework [1]. We see that HP Xe gas is able to diffuse freely into the LP environment at room temperature. At reduced temperatures both NP and LP forms coexist and Xe diffuses to both on different time scales. Fast exchange between the LP and NP forms suggests intimate connectivity of the two channels. Inter-particle exchange between different orientations of the NP crystallite is also present. Quantitative analysis of the kinetics of at both temperatures will be presented.

[1] M. A. Springuel-Huet et al., J. Am. Chem. Soc., 2010, 132,11599

Poster 147

An ‘Open-Source’ 129Xe Polarizer for Clinical Imaging, in vivo MRS/MRI, and NMR/MRI of Porous Materials

Peter Nikolaou1, 2; Aaron Coffey1; Laura L. Walkup2; brogan Gust2; Nicholas Whiting3; Hayley Newton3; Scott Barcus5; Iga

Muradyan6; Greg Moroz2; Matthew Rosen7; Samuel Patz6; Michael J. Barlow4; Eduard Chekmenev8; Boyd M. Goodson2;

1Vanderbilt Univ, Nashville, TN; 2Southern Illinois University Carbondale, Carbondale, IL; 3SPMMRC; U. of Nottingham, Beeston, UK; 4University of Nottingham, Nottingham, UK; 5Drake University, Des Moines, IA; 6Brigham & Women's

Hospital, Boston, MA; 7Harvard University, Somerville, MA; 8Vanderbilt Univ Institute of Imaging Science, Nashville, TN

We have constructed an "open-source" large-scale (>1 L/hr) 129Xe polariser for clinical, pre-clinical, and materials NMR/MRI applications. Comprised mostly of off-the-shelf components, our automated polarizer is easy to use and employs a simplified "open-source" design that will be readily implementable in other laboratories. Unlike most other clinical-scale Xe polarizers, our device runs with xenon-rich gas mixtures (up to 2000 Torr in 500 cc) in either single-batch or stopped-flow mode, in part negating the usual requirement to cryo-collect the hyperpolarised 129Xe (simplifying gas handling while eliminating polarization losses associated with freeze-thaw cycles). In-cell (during SEOP) Xe polarizations of ~70% and ~30% (calibrated with low-field 1H NMR) have been measured for Xe partial pressures of ~800 Torr and ~1600 Torr, respectively.

Poster 148

Surface Enhanced NMR by DNP: A Tool for Structural Investigation of Supported Catalyst Species

Moreno Lelli1; Aaron J. Rossini2; Alexandre Zagdoun2; David Gajan3; Gilles Casano4; Olivier Ouari4; Melanie M Rosay5; Werner E. Maas6; Paul Tordo4; Coperet Christophe3; Anne Lesage1; Lyndon Emsley2; 1ENS Lyon/CNRS, Villeurbanne,

France; 2ENS Lyon, Villeurbanne, France; 3ETH Zürich, Zürich, Switzerland; 4Aix Marseille University, Marseille,

France; 5Bruker BioSpin Corporation, Billerica, MA; 6Bruker Biospin, Billerica, MA

Dynamic nuclear polarization (DNP) is becoming a general method to enhance sensitivity of NMR experiments. We have recently applied DNP in MAS solid-state NMR to investigate organic functional groups on the surfaces of porous materials, introducing polarizing agent through incipient wetting impregnation. This approach is valid for many solvents, including organic solvents, and applicable to different materials, with 1H DNP enhancement that may reach two orders of magnitude. Here, we will report results obtained with surface enhanced DNP NMR on mesoporous hybrid materials used as catalyst precursors. The high DNP enhancement for 29Si and 13C nuclei cross-polarization experiments makes it possible to obtain structural information about the conformation of the organic tethers anchored on the silica surface.

Poster 149

Correlating in vivo Hyperpolarized 13C Spectroscopy with Physiological Parameters in the MMTV-PyMT Transgenic

Mouse



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Matthew E Merritt; University of Texas Southwestern Medical Center, Dallas, TX

The MMTV-PyMT Transgenic Mouse is a model of spontaneously occuring human breast cancer. We studied mice within 1 month of initial tumor appearance using hyperpolarized [1-13C]pyruvate as a metabolic imaging agent. Following jugular vein catheter injection of the imaging agent, [1-13C]lactate signal typically peaked at a time after the peak pyruvate signal. Plotting the time of maximum lactate signal (Tmax) versus a variety of physiological parameters revealed extremely strong correlations with [Lac] and the LDH activity, but not with tumor size. Due to large uncertainties, the [Pyr] and hence the [Lac]/[Pyr] ratio showed minimal correlation with Tmax. Despite this, the correlation with important in vivo parameters indicates the efficacy of using hyperpolarized spectroscopy to study this breast cancer model.

Poster 150

Observation of Strongly Forbidden Transitions via Electron-Detected Solid Effect DNP

Albert Smith; Bjorn Corzilius; Olesya Haze; Timothy Swager; Robert Griffin; MIT, Cambridge, MA

We present experimental results for which solid effect (SE) DNP was observed indirectly, via measurement of polarization loss on the electron. SE can be observed via polarization gain on the nuclei, or via polarization loss on the electron when the matching condition, δϊ0S=±ϊ0I, is satisfied (δϊ0S is the microwave frequency offset from the electron Larmor frequency, ϊ0I is the nuclear Larmor frequency). In our experiments, polarization loss on the electron was observed for δϊ0S=±nϊ0I where n=1,2,3,4. This was unexpected, since the most direct DNP pathways for n>1 are highly forbidden. We discuss the possible reasons for this observation. Also, we show that our results are consistent with our recent model of the spin-diffusion barrier and recent theoretical results.

Poster 151

A Tri-Enzyme System for Efficient Photo-CIDNP under Low-Photodegradation Conditions

Jung Ho Lee; Silvia Cavagnero; University of Wisconsin-Madison, Madison, WI

Photo-CIDNP is a powerful method to enhance NMR sensitivity in solution. Prolonged high-power laser pulsing during photo-CIDNP, however, tends to irreversibly damage the molecules of interest and reduce the effective concentration of the light-absorbing dye (typically FMN). Here, we introduce a novel tri-enzyme system that significantly overcomes the above challenges. Two enzymes effectively remove oxygen from the sample and one additional enzyme specifically re-oxidizes the reduced FMNH2 dye (replacing oxygen’s role). As a result, the new tri-enzyme system rescues the sample from oxygen-dependent photodegradation and efficiently regenerates FMN, improving long-term photo-CIDNP data collection. This approach can be applied to increase NMR sensitivity in photo-CIDNP experiments on very dilute samples and multidimensional photo-CIDNP data collection at high laser power.

Poster 152

Metabolism of Hyperpolarized [1-13C]Pyruvate in the Isolated Perfused Rat Lung – An Ischemia Study

Stephen Kadlecek1; Benjamin Pullinger, 1; Kiarash Emami1; Harrilla Profka1; Mehrdad Pourfathi1; Masaru Ishii2; Rahim

Rizi1; 1University of Pennsylvania, Philadelphia, PA; 2Johns Hopkins University, Baltimore, MD

Very few lung NMR studies have been reported due to low signal density arising from low tissue densityand line broadening from air-tissue interfaces. These difficulties can be partially overcome using fast-dissolution 13C-DNPNMR. This experiment studies the evolution of the [1-13C] lactate signal in the isolated, perfused rat lung after injection of[1-13C] pyruvate and fermentative glycolysis. The observed accumulation of lactate, which represents a combination of netmetabolic flux through LDH and label exchange between the pyruvate and lactate pools, is then studied under normoxicand ischemic states. In combination with 31P-NMR spectroscopy, 13C spectroscopy of hyperpolarized (HP) pyruvate is studied as a method tonon-destructively probe the redox state in lung tissue, as well as for its potential to acquire this information regionally.

Poster 153

Modeling T-1 and Spin Diffusion in Pure-xenon Clusters during 129Xe DNP

Mehrdad Pourfathi1; Nicholas N. Kuzma1; Huseyin Kara1, 2; Stephen J. Kadlecek1; Rahim Rizi1; 1University of

Pennsylvania, Dept. of Radiology, Philadelphia, PA; 2University of Pennsylvania, Dept. of Physics, Philadelphia,

PA Dynamic nuclear polarization (DNP) of 129Xe has spurred renewed interest in hopes of producing bulk quantities of highly polarized solid xenon. The reported 129Xe polarizations, however, vary widely in the previous DNP reports and are still considerably lower compared to 13C DNP. Here we develop a simple model that incorporates nuclear spin diffusion and T1 relaxation in the pure xenon clusters to account for the peculiar time evolution of the narrow 129Xe NMR peak observed in our experiment. Theoretical spin-up and spin-down curves calculated based on the basic microscopic DNP parameters can be fitted to the experimental data and thus provide a valuable local probe of the DNP process.

Poster 154

Dynamic Nuclear Polarization of 15N-enriched Laughing Gas

Nicholas N. Kuzma1; Huseyin KARA1, 2; Mehrdad Pourfathi 1; Philip Manasseh3; Rajat Ghosh1; Stephen J. Kadlecek1;

Giuseppe Pileio4; Pär Håkansson4; Malcolm Levitt4; Rahim R. Rizi1; 1University of Pennsylvania, Dept. of Radiology, Philadelphia, PA; 2University of Pennsylvania, Dept. of Physics, Philadelphia, PA; 3Department of Chemistry, Earlham College, Richmon, IN; 4School of Chemistry,

Southampton University, Southampton, Hampshire, UK An emerging development makes it possible to store polarization in the singlet states of a coupled two-nuclear-spin system with slightly different chemical shifts, such as doubly labeled 15N2O . Here, we demonstrate the first dynamic nuclear polarization (DNP) of 15N2O. We also report a dramatic change in the solid-state 15N2O NMR spectrum after warming the sample up to about 120 K over several minutes. We believe this leads to a spontaneous formation of pure 15N2O clusters in the N2O/1-propanol/trityl solid matrix. We present the effects of this pure-N2O cluster formation on DNP magnitude and polarization time constant in the solid 15N2O/1-propanol/trityl mixture.



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Poster 155 Cluster Formation in Solid-state Mixtures Restricts DNP

of 129Xe Nicholas N. Kuzma1; Huseyin Kara1, 2; Mehrdad Pourfathi1; Philip Manasseh3; Rajat Ghosh1; Jan H Ardenkjær-Larsen4;

Stephen J. Kadlecek1; Rahim R. Rizi1; 1University of Pennsylvania, Dept. of Radiology, Philadelphia, PA;

2University of Pennsylvania,Dept of Physics, Philadelphia, PA; 3Department of Chemistry, Earlham College, Richmon, IN;

4GE Healthcare, Brøndby, Denmark Recent reports of 129Xe dynamic nuclear polarization (DNP) spurred renewed interest in producing large quantities of highly polarized xenon for human-lung MRI. Compared to well-established 129Xe optical pumping schemes, DNP is performed in the solid state, with higher Xe density and, potentially, higher production rates. DNP requires an intimate mixture of the target (xenon) with the source of unpaired electron spins, e.g. a free-radical molecule. A glassing agent (1-propanol) is usually added to achieve a homogeneous mixture of the radical with the target substance. Glassing behavior, however, is difficult to predict and to control. To resolve these issues, we used 129Xe NMR spectroscopy with part-per-million (ppm) resolution as a local probe to investigate DNP in xenon/1-propanol/trityl-radical mixtures.

Poster 156

129Xe T1 Increases Due to Thermally-Activated Clustering of Xe Atoms in Solid-State DNP Mixtures

Huseyin Kara1, 2; Nicholas Kuzma2; Mehrdad Pourfathi2; Stephen J. Kadlecek2; Rahim RIZI2; 1University of

Pennsylvania, Dept. of Physics, Philadelphia, PA; 2University of Pennsylvania, Dept. of Radiology, Philadelphia, PA

Optical pumping of 129Xe is a well-established method for producing hyperpolarized Xe gas, but offers challenges in scaling up the production volume. On the other hand, recent reports show a potential for Dynamic Nuclear Polarization (DNP) to produce large volumes of hyperpolarized 129Xe in the solid state. In this study we investigated how T1 is affected by formation of pure-xenon clusters in xenon/1-propanol/trityl matrix. Exposing a homogeneously mixed sample to ~125 K temperature for several hours led to partial clustering of pure xenon in the solid matrix.

Poster 157

BDPA: An Efficient Polarizing Agent for Fast Dissolution DNP-NMR Spectroscopy

Lloyd Lumata1; S. James Ratnakar1; Ashish Jindal1; Matthew E Merritt1; Arnaud Comment2; Craig Malloy1; A. Dean Sherry1;

Zoltan Kovacs1; 1University of Texas Southwestern Medical Center, Dallas, TX; 2Ecole Polytechnique Federale de

Lausanne, Lausanne, Switzerland The free radical 1,3-bisdiphenyl-2-phenylallyl (BDPA) has an EPR linewidth D that is comparable to trityl OX063 and is thus an efficient polarizing agent in dynamic nuclear polarization (DNP) via the thermal mixing process. Although BDPA is hydrophobic, we have found that it is reasonably soluble with sulfolane and other glassing solvents (e.g. DMSO, methanol). Large NMR signal enhancements in the liquid-state were obtained for a number of hydrophobic (e.g. tetramethylallene, benzene) and hydrophilic compounds (e.g. 13C pyruvic acid, 15N choline). In addition, the hydrophobic BDPA radical naturally precipitated out in the dissolution liquid when water

is used as dissolution solvent and thus, could be removed easily by a simple mechanical filtration process.

Poster 158

Enhanced Efficiency of Dissolution Dynamic Nuclear Polarization

Sean Bowen1; Jan Henrik Ardenkjær-Larsen1, 2; 1Technical University of Denmark, Kgs. Lyngby, Denmark; 2GE

Healthcare, Brøndby, Denmark Dissolution DNP enables the high spin polarization obtained from DNP in the solid state at low temperature to be preserved during the transition to the solution state. In order to best make use of this enhancement, it is critical to maximize the efficiency of the dissolution in terms of sample recovery and solution state polarization. The ability to hyperpolarize large volume samples benefits both imaging and spectroscopy experiments. To accomplish this, we have designed a new large volume sample cup and dissolution head for the Hypersense DNP system. We show that these enhancements permit even large volume samples to be dissolved with high recovery and retention of polarization in the solution state.

Poster 159

Quantitative Analysis of High Field Liquid State DNP at 3.4 T

Jan van Bentum1; Gijs van der Heijden1; Piotr Kurek2; Han Gardeniers2; Arno Kentgens1; 1IMM, Radboud University,

Nijmegen, Netherlands; 2MESA+, Twente University, Enschede, Netherlands

We present a double resonance structure for high field DNP at 95 GHz and 144 MHz. A miniaturized radiofrequency coil is integrated within a single-mode non-radiative dielectric resonator. With this probe it is possible to perform double resonance experiments on nanoliter samples in which enhancement factors of up to -160 are observed. By combining temperature dependent NMR relaxation, EPR, and DNP experiments, we have shown that the Overhauser model is still valid at 3.4 T. Currently, a µ-RF coil sputtered on a 200 µm capillary in combination with in-situ shimming allow for quantitative analysis of ~10 nl samples with 0.2 ppm resolution. Ultimately, 13C detection will be included for a complete analysis and screening of e.g., metabolites or other biomarkers.

Poster 160

Solution NMR Studies of Parahydrogen-Induced Polarization Enhancement via SABRE

Ping He1; Kirsten Groome1; Eduard Chekmenev2; Boyd M. Goodson1; 1Southern Illinois University, Carbondale, IL;

2Vanderbilt University Institute of Imaging Science, Nashville, TN

We report investigations of polarization enhancement in solution by para-hydrogen via SABRE (Signal Amplification by Reversible Exchange), which utilizes a metal catalyst transiently bound to both pH2 and a target substrate. As demonstrated by Duckett et al., SABRE allows substrate hyperpolarization without permanent chemical alteration. Parahydrogen (~99%) is generated at Vanderbilt and lasts 2-3 weeks following transport. In-house synthesis of an N-heterocyclic carbene iridium complex (whose use for SABRE was demonstrated at York) permitted improved enhancements (>2 orders of magnitude at 9.4 T) versus



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commercial catalysts. While providing room for improvement, these initial results clear the way for ongoing efforts to explore novel SABRE experiments--including those investigating alternate conditions, substrate types, and catalysts for a variety of potential applications.

Poster 161

Hyperpolarized 129Xe Chemical Exchange Saturation Transfer Contrast Agents Based on Bacterial Gas

Vesicles Mikhail G. Shapiro1, 2; Richard M. Ramirez2, 3; Lindsay J.

Sperling3; George Sun2; Jinny Sun2; Alex Pines2, 3; David V. Shaffer2; Vikram S. Bajaj2, 3; 1Miller Research Institute,

Berkeley, CA; 2University of California, Berkeley, Berkeley, CA; 3Lawrence Berkeley National Laboratory, Berkeley, CA

Magnetic resonance imaging (MRI) contrast agents are useful in a variety of scientific and clinical applications. Most are designed to act on aqueous protons; however a new class of molecular imaging agents use 129Xe as an exogenous contrast medium. The properties of 129Xe can be leveraged in 129Xe contrast agents to exploit chemical exchange saturation transfer (HYPER-CEST), a signal amplification technique that takes advantage of 129Xe exchange between bulk solution and the contrast agent. We explore the potential use gas vesicles, which are intracellular, gas-filled nanostructures, as HYPER-CEST contrast agents. We report that gas vesicles, both in intact organisms and in purified form, interact with xenon gas, and that their presence can be detected using HYPER-CEST in a dose-dependent manner.

Poster 162

in situ Raman Mapping of Gas Temperatures in Spin-exchange Optical Pumping Cells for use in

Hyperpolarized Noble Gas NMR/MRI Nicholas Whiting1; Hayley Newton1; Michael J. Barlow1; Peter

Morris1; Boyd M. Goodson2; 1University of Nottingham, Nottingham, UK; 2Southern Illinois University, Carbondale, IL

We report in situ measurements of gas temperatures inside spin exchange optical pumping (SEOP) cells using Raman scattering from the Nitrogen quenching gas. Results include using high power, frequency-narrowed lasers pumping on the Rb D1 transition; earlier studies with broadband lasers show gas temperatures can be elevated to hundreds of degrees above ambient. We also correlate the measured gas temperature (with <1 mm3 spatial resolution) with in situ 129Xe NMR spectroscopy at various positions within the OP cell, under a variety of experimental parameters. This work should lead to an increased understanding of SEOP and improved production of hyperpolarized noble gases for use in MR applications.

Poster 163

Hyperpolarized 129Xe for Biological Applications Celine Boutin; CEA Saclay, Gif Sur Yvette, France

Hyperpolarized 129Xe NMR spectra of cells present two peaks: intra and extracellular compartments. Intensity and chemical shift of the downfield peak depends on the cell line, the integrity, the density and also on toxics. The slow exchange regime between both compartments gives access to the membrane permeability. Another strategy is to use a molecular system hosting xenon. The first in-cell probing of biological events using 129Xe NMR reveals the internalization of the biosensor. Dealing with smart biosensors, the chemical

shift of xenon caged in a cryptophane bearing a nitrilotriacetic acid arm allows the detection of Zn2+ at 100 nM. Preliminary MRI experiments have been performed on rats in which the biosensor is instillated previously to the inhalation of xenon.

in vivo NMR SPECTROSCOPY, 164 - 170

Poster 164

Accelerated Multi-Voxel Two-Dimensional in vivo Spectroscopy using Compressed Sensing

Jon Furuyama; Neil Wilson; Brian Burns; Rajakumar Nagarajan; M. Albert Thomas; Daniel Margolis; Steven

Raman; Nanette DeBruhl; UCLA, Los Angeles, CA The recently proposed Echo-Planar J-Resolved Spectroscopic Imaging and Echo-Planar Correlated Spectroscopic Imaging allow for the collection of four-dimensional (two spatial, two spectral) in vivo data. Both sequences are accelerated by the EPSI readout, which simultaneously interleaves the collection of one spatial and one spectral dimension. Despite the speed increase from the EPSI readout, the kyt1 plane still needs to be incrementally collected, requiring roughly 20-40 minutes of scan time. We show that Compressed Sensing can be used to reduce the 4D acquisition time by at least a factor of 3-4 by applying non-uniform under-sampling in the kyt1 plane.

Poster 165

in situ Membrane Protein Studies using 19F Site-specific Labeling and 19F Nuclear Magnetic Resonance

Changlin Tian; Univ. of Sci. & Tech. of China, Hefei, Anhui, China

The functional diversity of membrane proteins is determined not only by membrane proteins themselves, but also by their interactions with membranes. Native cellular membranes host various proteins, together with lipids in a variety of compositions in both leaflets. These heterogeneous membrane environments are known to influence conformational plasticity of membrane proteins, which is essential for their functions under native conditions. Here, an unnatural amino acid, trifluoromethyl-phenylalanine (19F-tfmF), was introduced to a membrane protein for site-specific side chain 19F chemical shift and relaxation rates measurements. Consequently, a new in situ method is presented to study the conformation and dynamics of membrane proteins in their native environment without further purification, using nuclear magnetic resonance.

Poster 166

in vivo Hyperpolarized Imaging of Hypoxia Inducible Factor-1 Activity in Murine Sarcoma

Ryan Davis; Duke University, Durham, NC Hypoxia inducible factor-1 (HIF1) is a nuclear transcription factor that regulates many cellular processes, including the conversion of glucose into cellular energy (ATP). HIF1 has received considerable attention in the field of cancer biology because in some cancer cells it shifts the flux of biochemical energy (i.e. pyruvic acid) away from cellular respiration in favor of increased lactic acid production. In this study, dynamic nuclear polarization of 1-13C-pyruvic acid, lactate spectral editing, and a HIF1 wild-type/knock-out murine sarcoma model are used to test if HIF1 knockout mice exhibit increased conversion of pyruvate to lactate and increased endogenous lactate levels relative to HIF1 wild-type mice.



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Poster 167 MRI of Black Widow Spiders

Brian Cherry; Gregory P. Holland; Dian Xu; Jeffery L Yarger; Arizona State University, Tempe, AZ

A long standing question has plagued researchers, how does a spider turn a protein-rich fluid into a very useful insoluble fiber, silk? Extensive work has been carried out to determine the bioplolymer structure responsible for the amazing properties of spider silk. However little is known on the exact mechanism the spider uses to transform the proteins into fiber. The dragline silk is comprised of two very large proteins that are stored in the major ampullate silk gland as a concentrated aqueous solution that is ~50% protein w/v. Magnetic Resonance Imaging and localized spectroscopy will be utilized to explore the protein state in vivo. Comparisons with ex vivo HRMAS studies on excised silk glands will be made.

Poster 168

Compressed Sensing in Selective Zero-Quantum Coherence Transfer (CS-SelZQC) Spectroscopic Imaging at Ultrahigh-Field without Susceptibility Artifacts and B0

inhomogeneous Broadening Qiuhong He1; Ying Sun2; Jeffrey Barker1; Song Chen1;

1University of Pittsburgh, Pittsburgh, PA; 2National University of Singapore, Kent Ridge, Singapore

Since the zero-quantum (ZQ) coherence spectrum obtained in the selective zero-quantum coherence transfer (Sel-ZQC) experiments is sparse, we have employed compressive sampling scheme in the ZQ evolution period in a Sel-ZQC experiment to image spatial distributions of polyunsaturated fatty acid (PUFA). A preliminary investigation has shown that a sampling reduction of 70% can be achieved without image deterioration. The ZQ spectroscopic imaging is insensitive to magnetic susceptibility artifacts and B0 inhomogenous broadening. As in Sel-MQC sequences, the unwanted lipid and water signals were dephased in a single scan – the CS-SelMQC method may be applied to study human breast cancer or other human diseases in extracranial organs containing high levels of mobile lipid.

Poster 169

Quantification of Cerebral Ketone Body Contents Elevated in the Streptozotocin-induced Diabetic Rat Brains using 1H Magnetic Resonance Spectroscopy

Ping-Chang Lin; Wen-Tung Wang; Phil Lee; In-Young Choi; University of Kansas Medical Center, Kansas City, KS

Diabetic ketoacidosis, which happens predominantly in those with type-1 diabetes mellitus, is a life-threatening complication and may lead to diabetic coma. Investigation of the connections between ketone bodies accumulated in brain is essential to comprehend ketoacidosis in hyperglycemic state. In this study, we identified acetone responsible for the peak observed at 2.22 ppm in the localized in vivo 1H MR spectra of rat brains in the condition of streptozotocin-induced hyperglycemia. Further, the levels of brain metabolites, including acetoacetate, acetone and β-hydroxybutyrate, were quantitated by using LCModel analysis of the corresponding MR spectra. We observed a high correlation between the levels of acetoacetate plus β-hydroxybutyrate and the level of acetone in the hyperglycemic rat brains.

Poster 170 Progressive Pathological Changes in Neurochemical

Profiles of the Olfactory Bulbs and Hippocampus of Tau Transgenic Mice (rTg4510)

Jieun Kim1; In-Young Choi1; Karen Duff2; Phil Lee1; 1University of Kansas Medical Center, Kansas City, KS;

2Columbia University Medical Center, New York, NY Tauopathies, characterized by pathologic aggregation of microtubule-associated tau protein and formation of neurofibrillary tangles, have been linked to neurodegeneration. In this study, we measured alterations in neurochemical levels associated with neuropathological processes of tauopathies in the hippocampus and the olfactory bulbs rTg4510 mice, using in vivo 1H MRS at 9.4 T. Longitudinal measurement of neurochemicals in the hippocampus from 5 to 12 months showed significant progressive changes in NAA, Ins, GABA, glutathione and glutamine. Neurochemical alterations in the olfactory bulbs preceded those in the hippocampus and were more pronounced at 5 months in rTg4510 mice, especially the levels of NAA and Glu. Results demonstrated regional susceptibility and progressive neuropathology of tauopathies and provide potential biomarkers of early neuropathological events.

INSTRUMENTATION, 171 - 187

Poster 171 Compact, Terahertz Gyrotrons Based on a Cryogen-free

Magnet for DNP-enhanced NMR Spectroscopy Thorsten Maly; Jagadishwar Sirigiri; Bridge12 Technologies,

Inc., Framingham, MA Gyrotron oscillators are the only known devices that fulfill the demanding criteria for DNP-NMR spectroscopy and their use has been demonstrated at NMR frequencies up to 700 MHz. However, for widespread proliferation of DNP-NMR, it is important to have turn-key instrumentation available that can be used even by non-experts in the field of THz technology. In this presentation we will discuss a novel, innovative design for compact, turn-key gyrotron systems, specifically designed for DNP-NMR. The device is based on a compact, cryogen-free magnet and the standardized design will allow operation between 198 and 527 GHz (300 – 800 MHz 1H NMR) with only minor modifications. A prototype tube is currently under development and we expect to present first experimental results.

Poster 172

A Completely Non-Resonant MR System Soumyajit Mandal1; Shin Utsuzawa1; Yi-Qiao Song2;

1Schlumberger-Doll Research, Cambridge, MA; 2Schlumberger, Cambridge, MA

As the name implies, MR is a resonance phenomenon. In particular, RF pulses can efficiently manipulate nuclear spins only if they are applied at the correct frequency, i.e., the Larmor frequency f0. The electronics used for detecting MR has also traditionally been designed to be resonant at f0. However, there is no fundamental reason for this constraint. In fact, making the MR electronics non-resonant has several advantages, including flexibility, robustness to coil loading, multi-nuclear operation, depth profiling in inhomogeneous fields, rapid frequency switching, and possible reduction of pulse ringdown time. We describe the design and



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implementation of a non-resonant magnetic resonance (NRMR) system. The unique capabilities of such systems are also illustrated using a range of NMR and NQR experiments.

Poster 173

J-coupling Measurements in Inhomogeneous Magnetic Fields

Soumyajit Mandal1; Yi-Qiao Song2; 1Schlumberger-Doll Research, Cambridge, MA; 2Schlumberger, Cambridge, MA

It is difficult to measure chemical shifts in the small and inhomogeneous magnetic fields found in ex-situ and single-sided NMR systems, such as those used in well-logging. However, we show that it is still possible to obtain chemical information from J-coupling constants, which are independent of static field strength and temperature.

Poster 174

Mobile Single-Sided NMR with Micro Structured Multilayer Coil Arrays

Jan Watzlaw; Jutta Müntjes; Wilfried Mokwa; Uwe Schnakenberg; Institute of Materials in Electrical Engineering,

Aachen, Germany Mobile single-sided NMR is a powerful tool but its main challenge is the inherently low signal-to-noise ratio (SNR) because of the reduced magnetic field strength and homogeneity. We therefore present planar micro structured coils in a novel multilayer assembly with an improved sensitivity due to the high density of turns that are close to the spins of interest. First CPMG measurements with a specially designed multi-channel NMR spectrometer and a comparison to a state-of-the art macroscopic coil show that the coils can either be used solely to measure a smaller volume with the same SNR or they can be arranged to form planar arrays to increase the field-of-view and to simultaneously improve either the SNR or the measurement time.

Poster 175

Construction of Magic-angle Spinning Probes for Lossy Biological Samples

Chin H. Wu; Christopher V. Grant; Stanley J. Opella; University of California San Diego, La Jolla, CA

We have developed technologies using both cross-coil [1] and single coil designs [2] that have the “low-E” characteristics to achieve low sample heating and improved RF field efficiency. In this poster, we discuss our effort to implement low-E technologies in magic angle spinning probes. We present the design and construction of a triple-resonance magic-angle spinning probe with 48 mm outer diameter. The performance measurements and the RF heating results will be presented and discussed. We will also present preliminary efforts toward the design and construction of a cross-coil MAGC design that fits into the same stator design.

Poster 176

Power-Efficient Broadband CPMG Excitation and Refocusing Pulses

Soumyajit Mandal1; Van Do2; Martin D. Hurlimann; Yi-Qiao Song3; 1Schlumberger-Doll Research, Cambridge, MA; 2Harvard University, Cambridge, MA; 3Schlumberger,

Cambridge, MA We have developed power- and energy-efficient broadband excitation and refocusing pulses optimized for the CPMG spin-echo sequence in an inhomogeneous static field.

Experimental results from multiple systems confirm our theoretical predictions. The new pulses produce an asymptotic signal-to-noise ratio (SNR) that is up to 3.25 times larger, in power units, than produced by rectangular excitation and refocusing pulses with the same peak RF amplitude and refocusing pulse length. We expect them to be broadly useful for NMR in inhomogeneous fields. In particular, we expect applications in stray-field and inside-out systems, such as those used for well-logging.

Poster 177

Solenoids Revisited: Improving Performance of Low-E Detection Coils

Peter L. Gor'kov1; Wenping Mao1, 3; Jason A. Kitchen1; Ivan Hung1; Michael E. Fey2; Wurong Zhang2; William W. Brey1; 1National High Magnetic Field Laboratory, Tallahassee, FL; 2Bruker BioSpin, Billerica, MA; 3Wuhan Institute of Physics

and Mathematics, Wuhan, PR China New variants of cross-coil Low-E resonators are examined in order to improve various aspects of biosolids probes performance. A “reverse-wound” detection solenoid is replacing conventional solenoid of the original Low-E design. It maintains similar B1 field profile at lower X/Y frequencies but reduces electric field E/B1 in the sample area. This new setup is appropriate for detecting medium-gamma nuclei (13C, 31P), resulting in 3.5X smaller sample heating at detection efficiency and no loss of efficiency. “Fused” Low-E resonators are introduced for shorter rotors/stators in order to eliminate arcing in confined space and to improve B1 homogeneity of X/Y channels. In fused resonator, 1H LGR and detection solenoid are connected to each other while their magnetic fluxes are still orthogonal.

Poster 178

'Shim-a-ring' Magnets - A Ring Magnet with a Coaxial Ferromagnetic Shim for Nuclear Magnetic Resonance Chaitanya Chandrana; Edwin Eigenbrodt; Jesse Resnick; David Dunkerley; David Platts; Pulak Nath; Los Alamos

National Laboratory, Los Alamos, NM We introduce a novel magnet assembly for Nuclear Magnetic Resonance (NMR). Unlike traditional designs (e.g. Halbach) that use precisely aligned multiple magnets to generate uniform magnetic fields, this design utilizes only two components - diametrically magnetized ring- shaped permanent magnet and a ferromagnetic co-axial shim. These two align themselves by magnetic attraction only. This low –cost assembly is automatable and scalable. It was designed using COMSOL 4.2a (COMSOL, Inc.). Prototypes were built using NdFeB magnets and low carbon steel. Magnetic field measurements with hall probes agreed with simulation results. NMR relaxometry was performed on water sample doped with CuSO4 using a 3.0 mm probe. This system will be used for measuring relaxation parameters influenced by magnetic nanoparticles in biological solutions.

Poster 179

Coil Adjustment for the Prevention of Higher Order Mode Interference in HTS NMR Probes

Jerris Hooker1; Arthur Edison2; William W. Brey1; Robert Nast4; Vijaykumar Ramaswamy3; Richard Withers4; 1National

High Magnetic Field Laboratory, Tallahassee, FL; 2UF/NHMFL, Gainesville, FL; 3University of Florida,

Gainesville, FL; 4Agilent Technologies, Santa Clara, CA



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When developing coils for use in a multi-resonant NMR probe it is very important to predict the locations of the higher order modes in the lower frequency coils. This research is based on a probe containing coils for 1H, 13C, 2H, and 15N at 600 MHz, 150 MHz, 92 MHz, and 60 MHz for a 14.1 T magnetic field. The 600 MHz 1H coil couples very efficiently to any modes in the other three coils near 600 MHz, which can interfere with tuning, matching, efficiency, and SNR of the 1H channel. The locations of the higher order modes can be adjusted by tweaking the coil characteristics in order to change the amount of dispersion in the mode spectrum.

Poster 180

A 250 GHz Gyrotron with a 3 GHz Tuning Bandwidth for Dynamic Nuclear Polarization

Alexander Barnes1; Emilio Nanni1; Qing Ni1; Sudheer Jawla1; Judith Herzfeld2; Richard Temkin1; Robert Griffin1; 1MIT,

Cambridge, MA; 2Brandeis University, Department of Chemistry, Waltham, MA

Designs and implementation of a novel tunable 250 GHz gyrotron oscillator for dynamic nuclear polarization (DNP) experiments with >10 W output power over most of a 3 GHz band and >35 W peak power are shown. The device can generate a substantial microwave field over the band used for DNP experiments, without the need for sweeping the NMR magnetic field. Substantially improved tunability is achieved by implementing a long (23 mm) interaction cavity that can excite higher order axial modes by changing either the magnetic field of the gyrotron or the cathode potential. The gyrotron was integrated into a DNP spectrometer, resulting in an enhancement of 54 on a membrane protein.

Poster 181

110 kHz MAS Yusuke Nishiyama; Yuki Endo; Takahiro Nemoto; JEOL

Resonance Inc., Tokyo, Japan The very fast magic angle sample spinning (MAS) above 110 kHz will be presented. The effects of strong dipolar interactions between 1H atoms are greatly reduced. This leads to enhancement of resolution, sensitivity, and T2 relaxation time. The long T2 relaxation time enhances signal intensity in 1H detected HMQC type experiments and in 1H double-quantum correlation experiments using the conventional INADEQUATE sequences. Very fast MAS also suppresses spin diffusion in 1H NMR of rigid solid. Spin diffusion among 1H spins are investigated by NOESY type exchange experiments.

Poster 182

Wireless High-Resolution NMR Spectroscopy on a Chip Herbert Ryan; University of Virginia, Charlottesville, VA

Wireless, inductively coupled resonators are integrated with microfluidic “Lab on a chip” devices to provide a cheap platform for high-resolution on-chip NMR spectroscopy. Our approach relies on planar rf resonators that are integrated into the microfluidic chip. These metal structures resonate at the Larmor frequency, and are coupled inductively to the NMR receiver. This mode of operation allows for easy insertion and removal of the microfluidic device from the spectrometer. We demonstrate that inductively coupled planar coils exceed the sensitivity of conventionally connected similar coils. Proton 1D and COSY spectra are presented to show that the sensitivity

and resolution offered by this approach are sufficient for high-resolution NMR spectroscopy.

Poster 183

A Millimeter Scale Implantable MRI Detector with Wireless Signal Amplifier

Chunqi Qian; Murphy-Boesch Joe; Der-Yow Chen; Stephen Dodd; Alan Koretsky; NIH, Bethesda, MD

An implantable coil containing an integrated parametric amplifier and coupled inductively to external loops has been constructed to provide enhanced localized sensitivity of internal tissue. The sample coil is one element of a double frequency resonator containing a zero-bias varactor that mixes the MR signal with an externally applied pump frequency to produce an amplified output at the Larmor frequency. The coil has been used to provide high resolution images of the kidney surface, enabling identification of micro-vascular structures of rat’s kidney in vivo.

Poster 184

Characterization of Doty 4 mm and 3 mmXC Probes Paul Ellis; George Entzminger; Doty Scientific, Columbia, SC

The intellectual driver behind this project was to characterize the S/N ratio for two Doty MAS probes (4 mm and 3 mm XC utilizing BMAX Decoupling coils) at room temperature. To accomplish this we determined the temperature increase as a function of spinning speed for the two probes. As a natural consequence of these measurements, we were able to determine the temperature gradient along the length of the rotor for each probe. Using α-glycine we determined the S/N ratio for both probes while spinning at 10 kHz. We report the S/N ratio, power settings, and pulse widths for both probes.

Poster 185

Simulations of the Electromagnetic Field in NMR Low-E Coils

Wenping Mao1, 2; Peter L. Gor’kov1; William W. Brey1; 1National High Magnetic Field Laboratory, FSU, Tallahassee,

FL; 2Wuhan Institute of Physics and Mathematics, C.A.S, Wuhan, China

The low-E coil consists of a loop-gap resonator (LGR) into which a solenoid coil has been inserted. As the continuation of our simulation work, we studied the low frequency channel of low-E coil and the total E-field during the cross polarization (CP) interval when the solenoid and LGR are driven simultaneously. The simulations show that placing the solenoid inside the LGR decreases 13C power efficiency by 3%, further reduces the E/B1 (by 10%), and leaves B1 homogeneity unchanged. Thus, the presence of the LGR does not significantly compromise sensitivity or homogeneity of the solenoid, and slightly reduces sample heating. Arcing is prone to occur at the areas between solenoid outer turns and LGR when high power applied.

Poster 186

Transverse Electromagnetic (TEM) Volume Coil for in vivo Imaging at 17.2 T

Eric Giacomini; Olivier Reynaud; Yoram Galinsky; Cyril Poupon; Denis Le Bihan; Luisa Ciobanu; CEA/DSV/I2BM/Neurospin, Paris, France

The radiofrequency (RF) coil design for magnetic resonance imaging at ultra high magnetic field (UHF) is challenging even



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for relatively small field of views required for preclinical imaging. The objective of this study was to design and build a transmit/receive volume coil for UHF. This goal was achieved by building a TEM coil operating at 17.2T. The coil was operated in passive transmit/receive mode using an in house built splitter/combiner circuit, which ensured a four-point excitation and the recombination of the signals on reception. We present homogeneity profiles obtained on phantom samples and report in vivo rat brain images. Our results show the feasibility of this coil prototype for small-animal imaging at UHF using standard pulse sequences.

Poster 187

NQR with an Ultra-Broadband MR System Soumyajit Mandal1; Yi-Qiao Song2; 1Schlumberger-Doll

Research, Cambridge, MA; 2Schlumberger, Cambridge, MA Traditional NQR spectrometers have to be re-tuned to handle different spectral lines or different compounds because every compound possesses a unique spectrum of NQR resonances. This issue limits the usefulness of NQR in practical applications such as detection of explosives and narcotics. We have recently developed an ultra-broadband (100 KHz – 3 MHz) magnetic resonance (NRMR) system that uses a completely un-tuned coil for both excitation and detection. We now show that it can be used to detect the NQR spectra of multiple chemicals with good sensitivity and no hardware retuning. The NRMR system provides major benefits in speeding up the NQR signal acquisition and also in using multi-frequency methods for better identification of chemicals.

INSTRUMENTATION/ LARGE SYSTEMS, 188 - 189

Poster 188

Spectrometer for Dynamic Nuclear Polarization at 700 MHz / 460 GHz

Evgeny Markhasin1; Alexander B Barnes1; Eugenio Daviso1, 2; Vladimir K. Michaelis1; Emilio Nanni1; Sudheer Jawla1; Paul

Woskov1; Ajay Thakkar1; Ronald DeRocher1; Judith Herzfeld2; Richard Temkin1; Robert Griffin1; 1Massachusettes Institute of

Technology, Cambridge, MA; 2Department of Chemistry, Brandeis University, Waltham, MA

We describe the design of a spectrometer for MAS DNP experiments at 700MHz/460GHz. Extension of DNP to 700MHz has required the development of probe technology, cryogenics, gyrotrons, and microwave transmission lines. The MAS DNP probe here contains a 460GHz overmoded corrugated waveguide and a cryogenic sample exchange system. Sample temperatures ≤85K result in improved DNP enhancements and are achieved by utilizing a novel heat exchanger design, stainless steel and brass vacuum jacketed transfer lines, and a bronze probe dewar. We have also implemented a nitrogen generation and drying system in series with a pre-cooling refrigerator that has reduced nitrogen usage by a factor of four. Preliminary enhancements are -40 and the microwave power dependence suggests the possibility for considerable improvements.

Poster 189

Counter-Current Heat Exchanger for Low-Temperature Solid-State NMR of Biological Molecules

Victoria L. Mooney; Suvrajit Sengupta; Elizabeth A. Fry; Kurt W. Zilm; Department of Chemistry, Yale University, New

Haven, CT

The importance of low-temperature, solid-state NMR has been shown for a number of biologically significant molecules. Low-temperature spectroscopy may be employed for several reasons, such as to enhance cross polarization efficiency by decreasing the mobility of protein moieties and to trap thermally stable intermediates of proteins with complex activation mechanisms. Here, we present a new variable-temperature, counter-current heat exchange system. This system may be used continuously over long periods of time, and so is ideal for NMR experiments involving biomacromolecules, which often require much signal averaging. In order to demonstrate the heat exchanger’s temperature range and stability as well as its usefulness in experiments involving large biological molecules, we collected spectra of a V49A bacteriorhodopsin mutant with 13C-labeled retinal.

LIQUIDS METHODS: BIOMOLECULES, 190 - 203

Poster 190

Implementing Non-Uniform Sampling and Iterative Reweighted L1-norm Regularization in “Intensity-critical”

NMR Experiments Shangjin Sun; Ranabir Das; R. Andrew Byrd; Structural Biophysics Laboratory, NCI-Frederick, Frederick, MD

When applying non-uniform sampling (NUS) for NMR experiments that encode structural or dynamic information (e.g. relaxation rates, RDCs, etc.) into modulation of the signal intensities, accuracy of the relative intensities is critical for accurately extracting the target parameter. We present our implementation of iterative reweighted L1-norm (IRL1) regularization, for applying NUS to relaxation rates and coupling constants measurements. Relaxation rates and coupling constants extracted from a series of IRL1 processed non-uniformly sampled data are within very small relative error from those extracted from the full data sets that are processed by Fourier transform. This fact indicates that one can attain the benefits of NUS (e.g. time saving, resolution and sensitivity enhancement) in intensity critical experiments.

Poster 191

Quantitative Characterization of the Structure of Plant Cell Walls with Time-zero Extrapolated 2D HSQC NMR

Spectroscopy Kun Cheng; Markus Pauly; Energy Biosciences Institute,

Berkeley, CA Lignocellulosic biomass is thought to be an upcoming renewable resource for the production of biofuels and other commodity chemicals. Lignocellulosics (plant cell walls) consist of cellulose, various hemicelluloses and lignin. Due to its structural complexity, analysis of lignocellulosics by NMR results in convoluted spectra. The present study investigates four different solvent systems (DMSO-d6, DMSO-d6/TBAF, DMSO-d6/[Hpyr]Cl-d6, and DMSO-d6/[Emim]OAc) for the solution-state 2D 13C-1H HSQC NMR characterization of plant cell walls (Miscanthus). DMSO-d6/[Emim]OAc completely dissolved cell walls and thus provided a higher-resolution NMR spectroscopy. The NMR analysis were supported by alternative analytical methods (GC-MS). Furthermore, the time-zero extrapolated HSQC NMR spectroscopy of Miscanthus walls was performed with [Emim]OAc-d14. The established NMR method enables



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quantitative understanding the structural traits of plant cell walls.

Poster 192

Structural Analysis of Human Plasminogen Peptide Interacting with Yersinia pestis Plasmin

Carolina Sarzedas; Thaís Vidal; Luiz Artur Chaves; Cristiane AnoBom; Luzineide Tinoco; UFRJ, Rio De Janeiro, Brazil

Yersinia pestis, the agent of “plague”, is classified as category A bioterrorism agent by CDC. Plague plasminogen activator (Pla) is an outer membrane protease (omptin) which is responsible for fibrinolytic and coagulase activities. In this work the peptide comprising the region of human palsminogen that interacts with Pla (PK2) was used as a model of palsminogen-Pla interaction. CD analysis shows that Pla promote structural modification in the PK2 spectrum. PK2 TOCSY spectra in the presence of Pla showed stronger cross peaks than the observed in the TOCSY of free PK2, indicating less flexibility for the PK2 interacting with Pla. This could be a useful model to designing mimetic peptides or to screening substances to inhibit this interaction.

Poster 193

Core of a Human Immunoglobulin Light-chain Variable Domain Amyloid Fibril Probed by Hydrogen/Deuterium

Exchange NMR Spectroscopy Simon Pondaven; The Ohio State University, Columbus, OH Deposition of variable domains of immunoglobulin light chains (Ig VL) as amyloid fibrils in vital organs and tissues, including the kidneys and heart, has been linked to the pathogenesis of light-chain amyloidosis, the most common systemic disease of this type in the Western hemisphere. Here we present the characterization of the core region for fibrils formed by a 114-residue human immunoglobulin light-chain variable domain, LEN, using DMSO-quenched hydrogen/deuterium (H/D) exchange combined with 2D HSQC solution-state NMR, and we compare these H/D exchange data to those recorded for LEN under native conditions.

Poster 194

Anomalous Relaxation in Aligned Bicelle Media Luke Arbogast; Joel R Tolman; Johns Hopkins University,

Baltimore, MD Measurement of chemical shift anisotropies (CSAs) by solution-state NMR has been plagued by difficulties, limiting their usefulness. For partial alignment methods that result in recovery of a residual CSA (rCSA), we have previously demonstrated in bicelles that significant media-dependent interferences contaminate measurements. To further elucidate the nature of these interferences we have investigated 1H/15N amide relaxation properties of the small protein GB1 in a strongly aligned bicelle environment. Comparison of relaxation parameters against those obtained in buffer show significant deviations. Specifically, the η/T2 ratio, which is sensitive to the CSA interaction strength and the T1/T2 ratio, which is sensitive to rotational correlation times, display deviations that are not easily explainable by changes in the rigid body rotational diffusion tensor.

Poster 195

The Properties of Galactolipids in Fast-tumbling Bicelles Weihua Ye; Stockholm University, Stockholm, Sweden

Bicelles as membrane mimetic systems are commonly applied for studies of membrane proteins. In this report, we describe new fast-tumbling bicelle systems with galactolipids incorporated. The integration of MGDG into the bilayer has been studied by NMR diffusion, which proved that the galactolipids are properly integrated into the bilayer. In addition, the dynamics of MGDG in the bilayer have been investigated by 13C relaxation. The combined results show that glactolipid containing bicelles may be applied for studying interactions between glycolipids and membrane protein glycosyltransferases.

Poster 196

Broadband Correlation Spectroscopy Pulse Design by Multi-Tilted, Multi-Rotating Frames

Paul Coote1; Haribabu Arthanari2; Gerhard Wagner2; Navin Khaneja1; 1Harvard School of Engineering and Applied

Sciences, Cambridge, MA; 2Harvard Medical Sch, Boston, MA We present a class of pulses for broadband or multi-band isotropic mixing at low power, suitable for protein spectroscopy, e.g. TOCSY and TACSY experiments. We demonstrate the crucial property of these pulses: for any scaler-coupled network of spins with chemical shifts in the active bandwidths, there exists a multi-tilted, multi-rotating frame of reference in which all effective chemical shifts are small and the effective coupling Hamiltonian remains large. That is, the Hartmann-Hahn mixing condition is satisfied. The ratio of radiofrequency power to chemical shift bandwidth for these pulses is much lower than for DIPSI, FLOPSY, and other mixing pulses. Carbon-channel TACSY experiments at low RF power support our theoretical analysis.

Poster 197

Fast Hyper-Dimensional NMR Spectroscopy of Short-Lived Biological Sample

Victor Zharavin1; Suhas Tikole2; Alexis Rozenknop2; Frank Löhr2; Vladimir Rogov2; Volker Doetsch3; Peter Güntert2, 3;

1Center for Biomolecular Magnetic Resonance, Frankfurt Am Main, Germany; 2Institute of Biophysical Chemistry, BMRZ, Frankfurt, Germany; 3Univ of Frankfurt, Frankfurt, Germany

We developed a fast NMR method using non-linear sampling and hyper-dimensional spectra processing. We optimized automated assignments using FLYA algorithm by varying peak-picking parameters to give the best S/N ratio for 3-30% NUS datasets. When varied the total number of experiments: a gradual increase in the number of assignments was observed. An improvement of the assignment was observed as a result of simultaneous processing. The results suggest a strategy to record a ‘maximal dataset’ with fixed total measurement time by lowering NUS ratios, to match protein lifetime (3 days for the cell-lysate samples). Overall, the approach allowed studying the structure, interactions, and function of ubiquitin-fused targets in native cell lysate without isolation and purification procedures.

Poster 198

Carbon Detected NMR Methods Probe Folding-Upon-Binding Events Involving Intrinsically Disordered

Proteins Scott Showalter; The Pennsylvania State University,

University Park, PA Intrinsically disordered proteins (IDPs) have poor 1H-amide chemical shift dispersion, so we have applied carbon-



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detection methods to their study. The intrinsically disordered C-terminus of FCP1 forms an amphipathic alpha helix when bound to RAP74 and we observe a partial helical character to the unbound ensemble. The disordered state of FCP1 is retained in the presence of macromolecular crowding agents and HeLa extract, but the extent of ordering can be controlled through the addition of osmolytes or chaotropes. Our NMR studies have been augmented by multiple microsecond simulations calculated using the purpose built ANTON machine. Our data suggest that the moderation of binding affinity associated with folding-upon-binding mechanisms may be generally less severe than previously indicated.

Poster 199

Gaining Sensitivity in Spin State Selection through IPAP Rasmus J. Linser; Gerhard Wagner; Harvard Medical School,

Boston, MA TROSY has been widely used to provide NMR characterization of large molecules. We show that its major drawback, the discarding of 50% of the initial magnetization, can be circumvented by using the concept of In-Phase/Anti-Phase (IPAP), which was originally designed for facilitated extraction of one-bond scalar couplings. Combining the two concepts, particularly for intermediate-molecular weight proteins a significant sensitivity gain can be achieved by TROSY-IPAP (“TRIPAP”), whereas a usual TROSY identical to standard recording can still be extracted. We show application towards TRIPAP backbone experiments and diagonal-free NOESY experiments, which result in a sizeable sensitivity increase and are reasonably easy to implement.

Poster 200

(4,3)D-HN (C)NH Experiment for Direct Sequential Connection of 1HN-15N HSQC Peaks In Labeled Proteins G Jithender Reddy; Tata Institute of Fundamental Research,

Mumbai, India We present here a NMR triple resonance pulse sequence, (4,3)D-HN (C)NH, and an approach derived therefrom for direct assignment of backbone amide resonance peaks in the 1HN-15N-HSQC spectrum of a protein. The reduced dimensionality concept employed in the pulse sequence, not only enhances information content of the 3D spectrum, but also enhances spectral dispersion, thereby enabling unambiguous identification of sequential correlations. The pulse sequence directly establishes correlations between1Hi, 15Ni, 1Hi+1 and 15Ni+1 spins by simultaneously encoding the 1HN and 15N chemical shifts during the t1 evolution period. The method has been demonstrated with 13C/15N-enriched Ubiquitin and also with M-Crystallin (Holo form).

Poster 201

Recent Advances in NMR Spectroscopy of Encapsulated Proteins in Low Viscosity Fluids

Nathaniel Nucci; Igor Dodevski; Joshua Wand; Univ of Pennsylvania, Philadelphia, PA

We continue to develop the reverse micelle technology for solution NMR studies of protein structure, dynamics and function. Reverse micelles are spontaneously organizing complexes of appropriate surfactants enclosing a small aqueous core dissolved in a non-polar ideally low viscosity solvent. Under optimized conditions, proteins can be encapsulated in the aqueous core of these complexes with structural fidelity. By using low viscosity solvents such as the

short-chain alkanes, these protein-containing particles can be made to tumble rapidly, permitting access to the techniques and experiments normally associated with small protein NMR spectroscopy. Here we will describe recent advances that allow efficient determination of encapsulation conditions, optimization of tumbling behavior in liquid ethane and investigation of hydration and other biophysical properties of proteins.

Poster 202

Perfecting WATERGATE: Suppressing J modulation Ralph W. Adams; Chloe M. Holroyd; Juan A. Aguilar; Mathias

Nilsson; Gareth A. Morris; University of Manchester, Manchester, UK

Water suppression, e.g. using WATERGATE, is a necessary component of many NMR experiments, particularly those involving proteins and metabolites. The J modulation that occurs during WATERGATE results in significant distortion of the signals in 1H NMR spectra making them difficult to interpret. We show how the WATERGATE sequence can be upgraded to incorporate a "perfect echo" rather than a spin echo. The perfect echo uses a quadrature π/2 pulse at the midpoint of a double spin echo to reverse the apparent sense of J modulation. In combination with WATERGATE this allows suppression of the solvent signal and, with the perfect echo refocusing the J modulation, removal of signal distortions. The sequence is demonstrated with solutions of protein, alcohols and sugars.

Poster 203

Optimized Relaxation Violated Coherence Transfer NMR Experiments for Estimation of Side-Chain Order in

Methyl-Protonated, Perdeuterated Proteins Vitali Tugarinov; University of Maryland, College Park, MD

We show that a 50% gain in the sensitivity of relaxation violated coherence transfer NMR experiments for estimation of side-chain order in [13CH3]-methyl-labeled, highly deuterated proteins, can be achieved through selection of methyl 1H triple-quantum (3Q) coherences. Such sensitivity gains are in contrast to expectations based on relative efficiencies of excitation of 2Q and 3Q coherences in AMX spin systems. The sensitivity gain is explained theoretically and verified experimentally on a number of protein systems with global rotational correlation times ranging from 10 to ~110 nanoseconds. In a collateral study, a 3Q-filtered relaxation violated coherence transfer scheme is developed where relaxation of multiple-quantum 1H-13C methyl coherence during the relaxation delay period is monitored.

LIQUIDS METHODS: SMALL ORGANIC MOLECULES,

204 - 225

Poster 204 Strategies for Structural Analysis using Pure Shift NMR

Juan Aguilar1; Julia Cassani2; Mathias Nilsson1, 3; Gareth Morris1; 1University of Manchester, Manchester, UK; 2Universidad Autonoma Metropolitana, D.F, Mexico; 3University of Copenhagen, Frederiksberg, Denmark

Pure shift NMR experiments1,2 are important new tools for structural analysis, simplifying the identification and characterization of structurally-related compounds. “Pure shift" spectra, in which all multiplet structure is suppressed, are



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particularly helpful in the analysis of complex mixtures, the greatly improved resolution afforded by broadband homonuclear decoupling allowing the identification of individual signals. We present results for the structural analysis of epimers of hesperidin and naringin, using a combination of constant time 3QF-COSY, TOCSY and ROESY experiments. 1. Aguilar, J.A., Faulkner, S., Nilsson, M., Morris, G.A. Angew. Chem. Int. Ed., 2010, 49, 3902. 2. Zangger, K., Sterk, H. J. Magn. Reson., 1997, 124, 486.

Poster 205

Determining Fatty Acid Aliphatic Chain Length by Isotropic Mixing

Joseph Sachleben; Ruiyang Yi; Paul Volden; Suzanne Conzen; Univ of Chicago, Chicago, IL

Lipids play critical roles in human health. Identifying fatty acids in a complex mixture from tissue extracts by nuclear magnetic resonance spectroscopy is a daunting challenge, because most saturated and unsaturated fatty acids have very similar NMR spectra. We are developing a technique, Aliphatic Chain Length by Isotropic Mixing (ALCHIM), to address this problem. CH2 chain length in fatty acids is measured with a selective TOCSY technique by the mixing time dependence of transfer to the other end of the CH2 chain. This technique is demonstrated on purified saturated and unsaturated fatty acids as well as lipid samples extracted from mouse adipose tissue. The possibility of using this method in mixtures of fatty acids of different lengths is also examined.

Poster 206

Fast access to Residual Dipolar Couplings by Single-scan 2D NMR in Oriented Media

Patrick Giraudeau1; Tobias Montag2; Benoît Charrier1; Christina M. Thiele2; 1Université de Nantes, Nantes Cedex 03,

France; 2Technische Universitat Darmstadt, Darmstadt, Germany

Measuring Residual Dipolar Couplings (RDCs) is highly useful for determining the structure of small organic molecules. However, the 2D NMR methods employed for such measurements are hampered by long acquisition times inherent to their incremental nature. Here, we present an original NMR method to measure 1DCH RDCs in a very short time, by ultrafast 2D NMR experiments performed for the first time in oriented media. An ultrafast coupled-HSQC is proposed to measure carbon-proton couplings in a single scan. It is applied to to isotropic and anisotropic isopinocampheol (IPC) samples, resulting in 0.2 seconds and 60 seconds total acquisition times, respectively. The dipolar couplings extracted from these experiments are in very good agreement with those obtained from their conventional counterparts.

Poster 207

Water mediated Nuclear Overhauser Effect: A New Approach to Investigate Clay-xenobiotics Interactions

Ronald Soong; Adolfo Botana; Andre J Simpson; University of Toronto, Toronto, ON

The enormous number of different xenobiotic substances in our environment is becoming a significant health concern. As these substances accumulate in our environment, the question of bioavailability becomes increasingly important. Clays, a major component of soils, are important in the

preservation of labile organics compounds. In the present work, we propose the use water-mediated NOE approach to probe the interactions between clay and pesticides . The Waterlogsy sequence will be used in our current studies to mediate the transfer of NOE from water to clay bound organics. Our results indicates this method is highly suitable in interrogating weak interactions in the fast exchange regime under the NMR time scales.

Poster 208

Analysis of Crude Reaction Mixtures from the Biotransformation of Sinapic Acid using

Matrix-Assisted DOSY Alberto Rodríguez1; Liliana Hernández-Vázquez1; Arturo

Navarro-Ocaña2; Hector Luna1; Julia Cassani1; 1Universidad Autónoma Metropolitana, D.F, México; 2Universidad Nacional

Autónoma de México, D.F., México The confirmation of the structure of different components present in mixtures produced by biotransformation processes usually needs the isolation of individual components. Even when the biotransformation with homogenated plants, where the enzimatic process are still activated, the results of reaction can not be one component and not always is the expected component1. Matrix-Asisted DOSY (MAD) NMR can assist in analyzing such mixtures, but the methodology has not been yet tested on this kind of mixtures. The present poster deals with the use of MAD to assist the analysis of the biotransformation of sinapic acid, via oxidative coupling reaction with peroxidases from Brassica oleracea and Opuntia ficus-indica. 1. Saliu, F. et al. Tetrahedron 2011, 52, 3856.

Poster 209

BASHD-J-Resolved-COSY: A New Method for Measuring Proton-Proton Spin Coupling Constants of Multiplet

Signals Kazuo Furihata1; Mitsuru Tashiro2; Haruo Seto3; 1University

of Tokyo, Tokyo, Japan; 2Meisei University, Hino, Japan; 3Tokyo Univ. of Agriculture, Tokyo, Japan

Natural products very often possess several spin systems consisting of a methine group directly linked to a methyl group (-CH-CH(CH3)-CH-). The methine proton splits into a broaden multiplet by coupling with several vicinal protons rendering analysis difficult of JH-H cross peaks of said methine proton in DQF-COSY or E-COSY. In order to overcome this problem, we have developed a new technique named BASHD-J-resolved-COSY. This method incorporates BASHD (BAnd Selective Homo Decoupled pulse) and J-scaling pulse into COSY. In this method, high resolution cross peaks can be observed in the F1 dimension by J-scaling pulse, and BASHD pulse collapses multiplet signals to simplified signals. Observation of JH-H values of multiplet signals becomes easy by introducing these two methods into COSY.



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Poster 210 Quantitative NMR Method for the Analysis of Neat

Chemical Weapon Materials David McGarvey1; William Creasy2; Suzanne Procell1; 1US

Army ECBC, APG, MD; 2SAIC, Aberdeen Proving Grnd, MD Chemical defense work in detection, personal and collective protection, decontamination and medical countermeasures requires high purity analytical standards of chemical weapon material. As a result, the U.S. Army established the Chemical Agent Standard Analytical Reference Material Program to provide well-characterized standards for research, testing and evaluation efforts. This research presents NIST-traceable quantitative analytical methods for the accurate analysis and characterization of super-toxic materials. These procedures minimize risk of exposure to the operators, while providing an accurate assessment of the absolute weight percent of the analyte in question. Identifying the structures of other components present in the sample is not required, and the presence of components undetectable by standard NMR methods (elemental sulfur, inorganic salts, etc) does not decrease the accuracy of the analysis.

Poster 211

15N-1H Double-Quantum Single-Quantum Correlation in Isotopically Unlabeled Organofluorine Molecules:

Evidence for C-F…H-N Hydrogen Bond Divya Kumari; Sankeerth Hebbar; Suryaprakash

Nagarajarao; Indian Institute of Science, Bangalore, India In organofluorine molecules the direct NMR spectroscopic evidence for the existence of C-F…N-H hydrogen bond is derived by the precise knowledge of signs and magnitudes of couplings, where the spin polarization is transmitted between the two coupled nuclei, both through covalent bonds and through space. The present study reports a two dimensional 15N-1H Double Quantum-Single Quantum correlation experiment, where 15N is present in its natural abundance, to obtain precise knowledge of the relative signs and magnitudes of 1hJFH, 3hJFH, 2hJFN and 1JNH to draw unequivocal conclusion on the existence of weak molecular interactions with organic fluorine.

Poster 212

Determination of The Absolute Configuration and Conformation of a New Vincamine Alkaloid. Combining

RDCs, DFT and Chiroptics. Pablo Trigo-Mouriño1, 3; Armando Navarro-Vázquez3; Roxana

Sifuentes2; Chakicherla Gayathri1; Helena Maruenda2; Roberto R. Gil1; 1Carnegie Mellon University, Pittsburgh, PA;

2Pontificia Universidad católica del Perú, Lima, Perú; 3Universidade de Vigo, Vigo, Spain

A new vincamine alkaloid 19-OH-(-)-eburnamonine has been isolated from Bonafusia macrocalyx. Its absolute configuration and conformation in solution has been determined by the combined use of DFT-DP4 chemical shift predictions,residual dipolar couplings and circular dichroism experiments.

Poster 213

Stereochemical Behavior of 77Se-1H Spin-Spin Coupling Constants in Pyrazolyl-1,3-diselenanes and 1,2-

Diselenolane

Leonid Krivdin; Yury Rusakov; Lyubov Papernaya; Alexandra Shatrova; A.E. Favorsky Irkutsk Institite of Chemistry, Irkutsk,

Russian Federation The derivatives of 1,3-diselenane are versatile intermediates in organic synthesis playing an important role in the development of organoselenium chemistry. Since the pyrazole cycle represents an important building block for the design of modern pharmaceuticals possessing analgetic, anti-inflammatory, anti-bacterial and anti-depressant activities, conformational studies of these molecules are of prime importance. A combined theoretical and experimental study of 77Se-1H spin-spin coupling constants in the series of the newly synthesized 2-(pyrazol-4-yl)-1,3-diselenanes together with related 1,2-diselenolane performed in this study revealed a marked stereospecificity of 2J(Se,H) and 3J(Se,H) couplings in respect with the geometry of the coupling pathway as well as the intramolecular interactions involving selenium lone pair which is of major importance for the stereochemical analysis of saturated selenium containing heterocycles.

Poster 214

Quantitative Metabolic Profiling of Body Fluids by Nonlinear Sampling and Forward Maximum Entropy

Reconstruction of 2D 1H-13C HSQC Neeraj Sinha; Ratan K Rai; Centre of Biomedical Magnetic

Resonance, Lucknow, India Two-dimensional (2D) NMR methods have shown to be an excellent tool for the identification and characterization of statistically relevant changes in low-abundance metabolites in body fluid. Although 2D NMR data provides large dispersions for peak assignment, aided in metabolite identifications and comprehensive metabolic profiling but it takes more time to collect the data, which make it inappropriate for metabolic profiling. We present the application of two – dimensional 1H-13C HSQC NMR spectroscopy for the quantitative metabolic profiling with reduction in the experimental time by non – linear sampling and FM reconstruction. Maximum Entropy Reconstruction and Non linear sampling techniques have been investigated for the quantitative metabolic profiling in body fluid.

Poster 215

Design, Construction, and Validation of a High Temperature Superconducting 13C-optimized 1.5-mm Cryogenically Cooled NMR Probe for Natural Products

and Metabolomics William W. Brey2; Arthur Edison1; Jerris Hooker2; Robert

Nast3; Vijaykumar Ramaswamy4; Richard Withers3; 1UF/NHMFL, Gainesville, FL; 2National High Magnetic Field,

Tallahassee, FL; 3Agilent Technologies, Santa Clara, CA; 4University of Florida, Gainesville, FL

Low sensitivity is the “Achilles’ Heel” of NMR. While 1H detection is advantageous from an NMR perspective, direct 13C detection would have several advantages for natural products and metabolomics. The problem is that 13C sensitivity is too low without hyperpolarization to be practical for many applications. We therefore designed a novel HTS probe optimized for 13C detection. The design goals were to minimize the sample volume for an optimal filling factor and sample quantity, optimize 13C performance without significantly compromising 1H performance, and utilize existing commercial probe body



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and cryogenic designs. The overall goal was a 10x increase in mass sensitivity beyond currently available probes. We will present details of coil design, optimization, and experimental measurements of probe performance.

Poster 216

Simple and Accurate Measurement of the Magnitude and the Sign of Small Heteronuclear Coupling Constants on

Protonated and Non-protonated Carbons Teodor Parella; Josep Saurí; UAB, Bellaterra, Spain

A proton-selective HSQMBC-TOCSY experiment is proposed to measure long-range proton-carbon (nJCH; n>1) coupling constants on both protonated and non-protonated carbons. The method combines in a single pulse scheme all the benefits known for the widely used HSQMBC and HSQC-TOCSY experiments. The magnitude and the sign of nJCH can be determined with excellent accuracy and great simplicity by analyzing the relative sense of the displacement of pure-phase IPAP multiplets in the direct dimension, showing particular interest to the application in the measurement of small J values on quaternary carbons.

Poster 217

Identification of Psychoactive Substances and Pharmaceuticals in Designer Drugs

Jerzy Sitkowski; Elzbieta Bednarek; Wojciech Bocian; Lech Kozerski; Zbigniew Fijalek; National Medicines Institute,

Warsaw, Poland Designer Drugs (DDs) problem emerged in EU several years ago. In the National Medicines Institute we have developed an orthogonal approach to assign the new chemical structures appearing on the market by means of applying complementary techniques, i.e. NMR, LC-MS/MS-TOF, GC-MS and powder X-ray diffraction which altogether allow to investigate the problem from different point of view as concerns the state of a drug, the separation of constituents and assignment of the new chemical structures appearing on the market over the years. Over 3750 various designer drugs and herbal highs products have been analyzed. About 90 compounds (55 psychoactive) were identified including: substituted cathinones, phenethylamines, synthetic cannabinoids, substituted phenylpiperazines, tryptamines, pharmaceuticals, and others.

Poster 218

Variable-Angle Assisted Scaling of Residual Dipolar Couplings in Small Molecules: Simultaneous

Determination of Conformation and Configuration Veera Mohan Rao . K; Jagadeesh Bharatam; Indian Institute

of Chemical Technology, Hyderabad, India The recent advent of stretched polymer gels as weakly aligned organic solvent media has added further impetus to the RDC-enhanced (NOE+RDC) NMR spectroscopy of small organic molecules and natural products at natural isotope abundance. Methods for attaining optimum spectral resolution by controlling the alignment strength of the polymer-gel, via mechanical compression and stretching are known. We employ a simple scaling method, variable–angle NMR (VA-NMR), to record linearly scaled multiple RDC data sets, for samples dissolved in a single alignment medium, that neither involve mechanical perturbation nor critical spinning of the alignment media. The RDCs recorded at various angles are least-square fitted. We demonstrate this

approach for identifying accurate conformation and configuration of small semi-rigid molecules with multiple stereo centres.

Poster 219

Exploring Three Injection Solutions using Multinuclear NMR Spectroscopy

Anthony A Ribeiro; Duke University, Durham, NC Injection solutions represent multicomponent mixtures of active pharmaceutical ingredient (API), buffers, isotonic agents and inert carriers. A previous paper described an NMR study on the degradation of Penicillin G [1]. Despite large signals from inert components in dexamethasone sodium phospahte, naropin (ropivacaine HCl) and epinephrine injection solutions, significant progress can be achieved in the NMR analysis of the API from multiple 1- and 2D 1H and 13C (COSY, TOCSY, HMQC, CIGAR) experiments. Our results inform on issues of drug stability, potential drug-drug interactions, neural toxicity and quality of manufactured injection materials. [1]. Mitsumori, Arata et al Bull Chem Soc. Japan 50:12 3164-6 (1977).

Poster 220

Anisotropic NMR Parameters and the Aggregation Behavior of Organometallic Compounds in Solution

Ann-Christin Pöppler; Georg August Universität Göttingen, Göttingen, Germany

Anisotropic NMR parameters are a versatile tool to gain information on the aggregation state of organometallics in solution. Because only few alignment media are compatible with this highly reactive material, we analyzed them in swollen polystyrene sticks. Thus we are able to discriminate between the different possible aggregates due to symmetry by measuring 1D NMR spectra of quadrupolar nuclei, e. g. 7Li. Providing stability of the samples for at least four weeks enables us to investigate methodological aspects (temperature and concentration dependence, stability, reproducibility and polymer characteristics). This technique was employed to a range of differently aggregated lithiumorganics in non-donating deuterated solvents.

Poster 221

Mixture Analysis with HR-MAS Pure Shift Selective TOCSY

Adolfo Botana; Andre J Simpson; University of Toronto, Toronto, Canada

The NMR identification of compounds in a mixture relies on being able to resolve the NMR signals for each compound. Unfortunately signal overlap is widespread in many mixtures. Pure shift methods allow increasing the resolution of NMR spectra by collapsing the multiplets into singlets. Here, it is shown for the first time that it is possible to run these methods in HR-MAS probes without further modifications. This is illustrated with a new pure shift experiment, the pure shift selective TOCSY, where the pure shift pulse sequence element is attached after a selective TOCSY. By exciting the anomeric protons in a mixture of sugars, a simplified picture is given of the correlations without the complications introduced by coupling splittings.



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Poster 222 No More Solvent Signals --- EXCEPT in One- and Two-

Dimensional NMR Spectroscopy Emmalou Satterfield; Missouri University of Science &

Technology, Rolla, MO Selective presaturation is a common technique to suppress large solvent signals that otherwise overpower and disturb the qualitative and quantitative analysis of dilute compounds. A new presaturation sequence, EXCEPT (EXponentially Converging Eradication Pulse Train), was found to be largely insensitive to variations in longitudinal relaxation times (T1) and radiofrequency fields (B1). To further suppress spurious solvent signals that remain after EXCEPT presaturation, we combined EXCEPT with W5-WATERGATE. The EXCEPT sequence was also applied to two-dimensional NMR experiments of aqueous solutions where H2O-signal artifacts can substantially obstruct the analysis of dilute compounds. For example, a significant improvement in the spectra quality was found for DQF-COSY experiments that were preceded by an EXCEPT presaturation.

Poster 223

Selective Multiple-quantum DANTE Clark D. Ridge1; Jamie Walls2; 1University of Miami, Coral Gables, FL; 2Department of Chemistry, Coral Gables, FL

By combining selective excitation with MQ-NMR, we can speed up the determination of the MQ-transitions which provide important structural information. Here we present a method for selectively exciting MQ-transitions based upon the MQ transition frequency and for "indirectly" detecting these transitions by observing changes to the z-magnetization. The selective excitation of MQ-transitions is obtained in a manner analogous to the DANTE pulse sequence. Where MQ transitions are not known a priori, they can be found by performing a series of experiments that scan the frequency of intrest. As the scanning method can be time-consuming, ultrafast multidimensional methods can be adapted to speed up aquisition. Theory and simulation are compared to experimental results for small molecules dissolved in liquid crystal solvents.

Poster 224

Generalization of Solvent Effects on One-Bond Indirect Coupling Constants

Astghik Shahkhatuni; Aleksandr Sahakyan; Aleksan Shahkhatuni; Henry Panosyan; Suren Mamyan; Molecule

Structure Research Center, Yerevan, Armenia The solvent induced variations of one-bond spin-spin coupling constants (SSCC) of several molecules dissolved in solvents with different polarity were investigated. The correlation of SSCC and dielectric permittivity of solvents was used to estimate the absolute values of SSCC devoid of intermolecular interactions by the linear extrapolation of SSCC values to ε0 dielectric permittivity of vacuum in “reaction field” coordinates. The obtained values found to be close to the values measured by gas phase NMR spectroscopy and/or predicted by quantum chemical calculations. The regression factors of these dependencies, showing the sensitivity of SSCC of each molecule to solvent polarity, were linearly correlated with the differences of their absolute values from one common value.

Poster 225 Quantitative NMR to Determine the Kinetics of the

Hydrothermal Degradation of D-glucose Lingyu Chi; Justin Cobb; Ariel Mollhagen; Douglas Ludlow;

Klaus Woelk; Rex Gerald; Missouri University of Science and Technology, Rolla, MO

Hydrothermal biomass-to-fuel reactions are a viable pathway for generating liquid biofuels. Currently, however, their yield and efficiency is low, and improvements are needed to make these reactions competitive with other methods of biomass conversion. Newly developed, quantitative NMR techniques are employed to identify reaction intermediates, understand the mechanisms, and study the kinetics of hydrothermal biomass reactions. The utilization of D2O as a solvent is compared with the application of a new solvent-signal suppression sequence, and internal and external references are tested for their reliability. The investigations are carried out in 10-mm NMR sample tubes with three cylindrical compartments so that the sample drawn from the reactive solution, the D2O lock, and the external reference are separated from each other.

LIQUIDS: NEW APPLICATIONS, 226 - 233

Poster 226

Function Prediction of Archeal Crystallin by High Resolution NMR Spectroscopy

Susmitha A L; Tata Institute of Fundamental Research, Mumbai, India

In the present context we detail out the application of NMR spectroscopy in characterizing not only the structure but also the function of a plausible eye lens protein ancestor. M- crystallin is a single domain archeal protein possessing characteristic paired Greek- key motif that binds Ca2+. Though its exact function remains elusive, this protein shares a vast structure similarity with that of two domain lens crystallins of higher organisms. Our NMR studies show that M- crystallin in single domain form exhibits enzymatic function while in two-mer form it exhibits domain interactions and behaves like an eye lens protein. Residue level characterization of partially denatured M- crystallin sheds light on protein aggregation and cataract formation in the human eye lens.

Poster 227

Strategies for Accurate Measurement of Long-Range 1H/X Scalar Coupling Constants

Ron Crouch; Agilent Technologies Research Products Division, Loveland, CO

There are a large number of experimental possibilities for measuring long-range heteronuclear coupling constants. Some 2D techniques are based upon HSQMBC for measurement with some computational fitting from F2 and others such as EXSIDE directly access values for coupling constants in F1. With modern instrumentation probes even very old experiments such as F1 band-selected Hetero 2D J spectroscopy can be quite convenient and time-efficient because of the compressed nature of the required F1 spectral window. Finally, a combination of multi-band F2 homo-decoupling and F1 band-selection has the potential to reduce the measurement of couplings to a single one dimensional experiment. In this poster various existing methods will be



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compared and novel strategies for measuring long-range heteronuclear coupling constants discussed.

Poster 228

Frequency-Swept CPMG for NMR Well-Logging Applications

Leah Casabianca; Daniel Mohr; Lucio Frydman; Weizmann Institute of Science, Rehovot, Israel

NMR has become an integral tool in well-logging applications. In the well-logging environment, T1 and T2 measurements are made to extract information about porosity, permeability, and the composition of fluids present in rock surrounding the well bore. In this work we show that by replacing the hard excitation and refocusing pulses of the CPMG sequence with frequency-swept or chirped pulses, we can excite a larger bandwidth and thus increase the resulting signal-to-noise of the CPMG experiment for a given rf power level. Hence frequency-swept pulses can be used in CPMG sequences to decrease experiment time in experiments with limited rf power and/or highly inhomogeneous environments such as those used in well-logging.

Poster 229

NMR at Ultra-Low Magnetic Fields - New Approach to Chemical Shift Analysis?

Szymon Pustelny; University of California at Berkeley/Jagiellonian, Berkeley, CA

We report on investigation of ultra-low magnetic-field NMR using optical magnetometry and prepolarization technique. This new approach allows us to observe NMR lines of ~10-mHz linewidth without application of spin echo. With signal-to-noise ratio of about 100, the position of NMR lines may be determined with a precision of 150 µHz without any averaging. It opens an avenue for application of the technique in detection of chemical shifts in the pT magnetic-field range. Such measurements are possible due to unique mechanism enabled by scalar spin-spin couplings between nuclei. The couplings provide dispersion of NMR lines in ultra-low magnetic field. Progress toward demonstration of chemical shift at ultra-low magnetic field is discussed.

Poster 230

Theory and Application of Pathway Selective Pulses Jamie Walls; Department of Chemistry, Coral Gables, FL

Recently, we introduced pathway selective pulses (PSPs) that excite a system only if certain evolution pathways are available. In designing a PSP, perfect time-reversal is often required, which, unfortunately, can only be achieved in simple systems. In this work, we apply PSPs to more complicated spin systems where the effects of imperfect time-reversal due to homonuclear couplings, field inomogeneity, and relaxation will be examined, and we compare are theoretical limits to the observed experimental results. Finally, we examine the effects of relaxation during the PSP, where line-narrowing under the PSP was observed in 13C labeled sugar samples for PSPs based on the INEPT sequence.

Poster 231

An NMR Investigation of the Nature of the Site-Specific Environmental Interactions Between Organofluorine

Compounds and Humic Acid James Longstaffe; Denis Courtier-Murias; Ronald Soong;

Andre J Simpson; University of Toronto, Toronto, ON

The organic material in soils and sediments plays a pivotal role in their environmental functionality, particularly with regard to the retention of important nutrients and organic contaminants alike. It has previously been shown that several organofluorine compounds exhibit specific interactions with humic acid (HA) that are not accounted for by phase-partitioning models. The work in this poster aims to elucidate the mechanisms contributing to these site-specific interactions using NMR spectroscopy. It is argued using temperature dependent PFG-diffusion measurements that perfluorooctanoic acid interacts with humic acid material only at conformationally restricted sites in remnant proteinaceous material. Using 1H{19F} RHSTD it is shown that the site-specific interactions of aromatic organofluorine compounds are most likely T-shaped interactions at electron deficient aromatic rings.

Poster 232

NMR Characterization of Self-inclusion Complexes of Nitrone Appended Macrocyclic Hosts

Roselyne Rosas1; Stéphane Viel2; Egon Rizzato2; David Bardelang2; Micaël Hardy2; Olivier Ouari2; Paul Tordo2;

1Fédération des Sciences Chimiques de Marseille, Marseille , France; 2Aix-Marseille Univ. & CNRS, ICR UMR 7273,

Marseille, France Nitrone-type spin traps are often used in spin trapping experiments to evidence the presence of free radicals. Recently, the spin trapping properties of these systems in aqueous solution have been shown to be significantly enhanced by grafting the nitrones to macrocyclic hosts, such as β-cyclodextrins (CD). However, the role played by several parameters (bridging arm length, nitrone size, nitrone hydrophobicity…) still remains to be explored. Three distinct CD appended nitrones were thus synthesized and studied by NMR. For all systems, ROESY allowed the position of the nitrone relative to the CD cavity to be investigated intramolecularly. ROESY data also showed intermolecular contacts that suggested the formation of self-included supramolecular assemblies involving several nitrone appended CD, as confirmed by DOSY experiments.

Poster 233

Simple Three Components Chiral Derivatizing Protocols for NMR Spectroscopic Enantiodiscrimination of Hydroxy

Acids, Primary Amines and Diacids Sachin Chaudhari; Bangalore, India

The three component chiral derivatization protocols have been derived for 1H and 19F NMR spectroscopic discrimination of a series of chiral hydroxy acids by their coordination and self-assembly with optically active α-methylbenzylamine and 2-formylphenylboronic acid. The chiral diacids have also been discriminated by their coordination and self-assembly with optically active α-methylbenzylamine and 2-formylphenylboronic acid or its derivatization with 3-flouro-2-fluoromethylboronic acid and α-(R)-methylbenzylamine. In addition the optically pure (S)-mandelic acid or trans-1, 2-Cyclohexanedicarboxylic acid in combination with 2-formylphenylboronic acid permits visualization of enantiomers of primary amines. The results derived on large number of systems using these protocols will be discussed.



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MATERIALS, 234 - 240

Poster 234 Thermal Degradation Studies of Poly (ethylene glycol)

Jian Wu; Tianlan Zhang; Miroslav Janco; The Dow Chemical Co., Spring House, PA

Polyethylene glycol (PEG) is widely used as a carrier for drug formulation and cosmetics, as well as in surfactant application. The mechanism of thermal oxidation of PEG and subsequent polymer chain scission were discussed extensively in literature. Some discrepancies are noted on how and where the polymer chain breaks down. In this study, we have characterized the thermal degradation (110 °C in atmosphere) product of a PEG (Mn~8K) by two-dimensional NMR, MALDI-TOF Mass spectroscopy and Size Exclusion Chromatography (SEC). Our analytical data suggest two competing degradation pathways occur simultaneously with the formate and ester species generated by chain cleavage and dehydration, respectively.

Poster 235

Solid-State NMR of Polymers under Mechanical Stress Ute Böhme; Ulrich Scheler; Leibniz-Institut für

Polymerforschung Dresden e.V., Dresden, Germany The effect of uniaxial stress on the molecular dynamics in polymers is investigated in low-field NMR while stretching the samples. The slower chain dynamics, which is most affected, strongly influences T2 and T1rho. Double quantum signals are pronounced in structures not containing CH3 groups. In elastomers any change of the molecular dynamics is instaneous and reversible. In semicrystalline polymers time-dependent effects are observed as well. To study these a new stretching apparatus for in-situ NMR studies has been built. T2 measured in a CMPG experiment is fasted and thus best suited for time-dependent experiments. The time dependence of T2 under constant elongation corresponds to that of the modulus indicating creep of the polymer as a source of stress relaxation.

Poster 236

Investigation of Ionic Liquids using Electrophoretic NMR Zhiyang Zhang; Jianbo Hou; Louis A Madsen; Virginia

Polytechnic Institute and State Universit, Blacksburg, VA Ionic liquids (ILs) are potential next-generation electrolytes in electrochemical devices due to their high ionic conductivity, negligible vapor pressure, and chemical and thermal stability. Transport behaviors of both cations and anions regulated by inter-ionic interactions drive the conductivity of ILs, thus affecting the performance of IL-based devices. Electrophoretic NMR (ENMR) is unique in that it measures the driven ion mobilities of both cations and anions using spectral separation. We present a new sample cell based on a conventional NMR tube that can successfully measure IL electrophoretic mobilities using a convection-compensated ENMR pulse sequence. We will discuss ionic transport phenomena in ILs and implications for electrolyte conduction mechanisms.

Poster 237 NMR Structural Studies of Peptide Hydrogel h9e and Relations of Their Physical Properties and Peptide

Monomer Structure

Hongzhou Huang1; Alvaro I Herrera1; Zhiping Luo2; Xiuzhi Sun1; Om Prakash1; 1Kansas State University, Manhattan,

KS; 2Texas A&M, College Station, TX We studied the self-assembly pathways and potential applications as a novel biological material of a recently designed hydrogel forming peptide FLIVIGSIIGPGGDGPGGD (h9e) from the rational combination of the sequences from human muscle L-type calcium channel (FLIVIGSII) and β-spiral motif of spider flagelliform silk protein (GPGGX)n. We determined the peptide monomeric structure by 2D 1H-1H NMR and studied its morphological and mechanical properties. Nanofiber morphologies appear at DMSO:H2O ratios smaller than 4:1. Increase of water in the solution induces a conformational change in the monomer, and enhances hydrogelation rate and gel strength. At the same DMSO:H2O ratios, adding Ca2+ not only promotes hydrogelation and gel strength but also confers special shear thinning and recovery properties without change of the monomeric conformation.

Poster 238

Transport and Structure in Electrolytes for Lithium Ion Batteries using Variable Temperature Diffusion and Spin-

Lattice Relaxation (T1) NMR Measurements Charles N. Adelson; T. Andrew Mobley; Leslie J. Lyons;

Grinnell College, Grinnell, IA 1H, 7Li, 11B Spin-lattice relaxation times (T1) and 1H, 7Li, 19F, and 11B diffusion measurements (D) were obtained for multiple types of alkylsilane oligo(ethylene oxide) lithium salt electrolytes. The effects of solvent structure, cation and anion identity, and salt concentration were explored with respect to the temperature dependent behavior of T1 and D. This paper will present our methodology and findings with respect to solvent structure, solvent/cation interactions, and cation/anion diffusivity as it relates to electrolyte usage in lithium ion battery development.

Poster 239

Angular Dependent Solid State 13C NMR Spectra of NR, PB, and PIB

Masashi Kitamura; Yoshiaki Hata; Hiroshi Yasuoka; Takuzo Kurotsu; Atsushi Asano; National Defense Academy,

Yokosuka, Japan Static 13C NMR spectra of natural rubber (NR), polyisobutylene (PIB) and polybutadiene (PB) after MAS were measured. We found that isotropic peaks become anisotropic after MAS. Because rubbers are easily deformed by MAS due to its relatively large centrifugal pressure, the anisotropic NMR spectra imply that the deformed rubbers have regularly aligned molecular chais. To clear the direction of the molecular orintation and how the orientation affects the 13C NMR spectra, we observed the angular dependent 13C NMR of the three rubbers after MAS. The magneteic susceptibility measurement was empolyed to elucidate the angular dependent 13C NMR spectra. The magnetic susceptibility change indicated that the electrons of the double bond in oriented chains also relate to the chemical shift.

Poster 240

NMR Characterizations of Metal-organic Frameworks Xueqian Kong1; Joseph Chen2; Hexiang Deng2; Fangyong Yan3; Jihan Kim3; Eric Scott2; Omar Yaghi4; Jeffrey Long2;

Berend Smit2; Jeffrey Reimer2; 1Environmental Energy



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Technologies Division, LBNL, Berkeley, CA; 2College of Chemistry, UC Berkeley, Berkeley, CA; 3Material Science Division, LBNL, Berkeley, CA; 4Molecular Foundry, LBNL,

Berkeley, CA Metal-organic frameworks (MOFs) represent a new class of synthetic solids that bring along record-setting porosity, as well as tunable pore sizes and surface chemistry. These frameworks show great promise in gas storage and separation such as CO2 capture and H2 storage. We use solid-state NMR to provide full-scale and in-depth characterization of MOFs i.e. their local heterogeneous structure, dynamics of adsorbed gas molecules, and high-throughput screening of surface area. The results offer clear guidance to computer simulation and predicted synthesis of MOFs for CO2 capture. A novel high-throughput device has been built as a potential alternative for industrial-scale quality control of porosity.

METABOLISM, MIXTURE ANALYSIS & STATISTICS, 241 - 254

Poster 241

Blind Source Separation Processing of Highly Overlapping DOSY Datasets

Ichrak Toumi1; Stefano Caldarelli1; Bruno Torresani2; 1Aix-Marseille Université ISm2, Marseille, France; 2Aix-Marseille

Université LATP CMI, Marseille, France Blind source separation is a general, non-parametric paradigm for un-mixing complex signals. The general concept is the following: observed signals are assumed to be linear combinations of unknown source signals. For the NMR spectrum of a mixture, the sources are the pure compounds signals. The prerequisite for a separation is that a series of measurements is available in which the individual sources vary differently. In this contribution, we demonstrate Non-Negative Matrix Factorization and Independent Component Analysis on DOSY datasets of oligosaccharides. This latter is a particularly challenging case, due to the very high level of spectral overlap, tantamount a reduced source independence. The sensitivity of the two algorithms to the relevant parameters for a successful demixing will be illustrated.

Poster 242

1H-NMR Metabolomics Studies on Lungs of Mice Exposed to Cigarette Smoking

Ju Feng; PNNL, Richland, WA In this work, liquid state 1H-NMR metabolomics and principal components analysis (PCA) were carried out to study the changes of metabolites in lungs of mice exposed to cigarette smoking. It was found that the concentration of adenosine was statistically significantly decreased but its metabolite inosine was elevated in the lungs exposed to cigarette smoking compared with controls, predicting deaminases were altered in lungs of mice exposed to smoking. Indeed, further gene screen confirmed that the adenosine monophosphate deaminase 2 (Ampd2) was up-regulated and the adenosine deaminase 2 (Adat2) was down-regulated in the lungs exposed to smoking. The investigation provided insight into the mechanisms of lung injury by cigarette smoking and identified that the purineric signaling pathway was affected.

Poster 243 Comparing Choline Compounds Levels in a Prostate

Tissue using 1H HR-MAS NMR Spectroscopy Alviclér Magalhães1; Homero J. F. Melo2; Jacob Szejnfeld2;

1IQ UNICAMP, Campinas, Brazil; 2RM/DDI, UNIFESP, Sao Paulo, Brazil

Non invasive techniques are being explored for a "watchful waiting" approach to prostate cancer patients to avoid aggressive treatment. MRI and MRSI using the mathematical relation total choline + creatine/citrate > 3SD have been increasing importance to evaluate prostate cancer (1, 2) unfortunately these methods carry a large number of false-positive. HR-MAS NMR spectroscopy, a nondestructive technique can be applied to intact tissue samples prior to quantitative histopathologic and immunohistochemical analysis, providing a direct correlation between metabolism, tissue type, and the underlying causes of the observed metabolic changes.(3) Few studies(3-5) use a mathematical relationship to evaluate ex-vivo HR-MAS NMR spectroscopy for characterization prostate tumors. Our results compare the choline compounds levels to citrate using HRMAS NMR in prostate biopsy specimens.

Poster 244

New Approaches for Complex Mixture Analysis Fengli Zhang; Kerem Bingol; Lei Bruschweiler-Li; Rafael

Bruschweiler; Florida State University & NHMFL, Tallahassee, FL

The detailed characterization of complex mixtures of biological molecules is critically important in the molecular life sciences including metabolomics. We have developed new homonuclear and heteronuclear NMR approaches to streamline the analysis of complex mixtures in combination with our public suite of COLMAR web servers (http://spinportal.magnet.fsu.edu), which perform covariance processing, spectral deconvolution, and database query. The new methods will be demonstrated for mixtures of different complexity.

Poster 245

Metabonomic Study of Host-phage Interaction by 1H NMR and STOCSY Based Analysis

Kanchan Sonkar; Rudra N. Purusottam; Neeraj Sinha; Centre of Biomedical Magnetic Resonance, Lucknow, India

We present a method for the qualitative and quantitative study of transient metabolic flux of phage infection at molecular level. The method is based on Statistical Total Correlation Spectroscopy (STOCSY) and PLS-DA applied to 1H NMR metabonomic data sets. The method has been implemented on 1H NMR data sets of growth media in planktonic cultures of Pseudomonas aeruginosa infected with bacteriophage pf1that has broad host specificity in P. aeruginosa. It has become increasingly recognized as an emerging opportunistic pathogen of clinical relevance due to antibiotic resistance via biofilm formation. Metabolic versatility of P. aeruginosa is considered to very important factor for its ecological succession, thus making it crucial to study the metabolism of P. aeruginosa.

Poster 246

Robust Information Recovery for Statistical Spectroscopy Lisa Vingara; David Gibbs; Armand Bankhead III; Eilis

Boudreau; Oregon Health and Science Univ., Portland, OR



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Statistical spectroscopy has become an important tool for NMR-based metabolomics research. One major obstacle in reaching its full potential is the computational demands of calculating every pairwise correlation between ppms of a high-resolution NMR dataset that can contain over 10,000 data points per spectra. In addition to computational time, viewing and extracting valuable information from such a large matrix is a nontrivial task. We approached this problem with bioinformatics tools to make the problem parallelizable and to extract important information. We demonstrate our approach on a set of 50 simulated NMR profiles containing 31 metabolites commonly found in human urine. We successfully extracted robust compounds arising from both inter- and intra- metabolite correlations.

Poster 247

Tailoring 1H Spin Dynamics in Small Molecules via Supercooled Water – A Promising Approach for

Metabolite Validation and Identification Hashim Farooq; Ronald Soong; Denis Courtier-Murias; Andre

J Simpson; University of Toronto, Toronto, Canada Metabolic mixtures are very complex and have considerable overlap of resonances when analyzed via NMR spectroscopy. This results in assignments that are sometimes ambiguous given the range of current NMR methods available. De novo molecular identification in these mixtures is generally accomplished using chemical shift information and J--coupling based experiments to determine spin connectivity information but these techniques fall short when a molecule of interest contain non-relaying centers. A method is presented here that uses the spatially-derived NOE, enhanced by a supercooled water solvent, to produce more complete spin systems and in turn subedit mixtures. This technique is applied to a standard mixture with overlapping resonances and is further demonstrated to assign molecules in a worm tissue extract.

Poster 248

NMR Based Metabonomics Study of NPY Y5 Receptor Activation in BT-549, a Human Breast

Carcinoma Cell Line Miki Watanabe1; Sulaiman Sheriff3; Junho Cho2; Kenneth

Lewis2; Ambikaipakan Balasubramaniam4; Michael A. Kennedy2; 1Claflin University, Orangeburgh, SC; 2Miami University, Oxford, OH; 3University of Cincinnati Medical

Center, Cincinnatti, OH; 4Cincinnati Veterans Affairs Medical Center, Cincinnati, OH

In Y5 receptor (Y5R) expressing BT-549 cells, neuropeptide Y (NPY) induced cell proliferation that was blocked by Y5R-selective antagonist CGP1683A (CGP). NMR-based metabonomics was used to monitor the metabolic profile of BT-549 cells in the presence of NPY and CGP to assess the effect of Y5R activation and inhibition during NPY induced cell proliferation. 1D 1H-NMR spectra of both hydrophilic cell extracts and growth medium were recorded from BT-549 with three treatments: NPY, CGP, and CGP followed by NPY. Alterations of seven metabolites upon the treatments were identified. Results indicated that Y5R activation induces cell proliferation by increasing the rate of glycolysis, glutaminolysis, and TCA cycle. In addition, the inhibition of Y5R by CGP counteracts NPY-induced changes in cellular metabolites.

Poster 249 NMR in Disease Diagnosis and Treatment Monitoring and

Functional MRI Studies on Meditation Cl Khetrapal; Dinesh Kumar; Uttam Kumar; Ashish Gupta; Lakshmi Bala; Center of Biomedical Magnetic Resonance,

Lucknow, India Utility of NMR in providing specific markers for diagnosis of and intervention in diseases of liver and bacterial infection is demonstrated. The metabolic profiles of urine and serum of liver-transplant patients is described with emphasis on possible causes of casualties. Diagnosis of urinary tract infection is presented with emphasis on the specificity of the bacteria giving rise to the infection. Changes in the metabolic profile of bile in patients with jaundice and colangitis and role of decompression therapy in obstructive jaundice are illustrated. The fMRI studies establish that meditation and ‘Mantras’ improve concentration and help in controlling emotions. They help in understanding effects of ‘Mantras’ and meditation on human behavior and provide valuable opportunities of societal relevance.

Poster 250

The Metabonomic Research on EGFP Transgenic Mice Hongde Li1; Hong Wei2; Dana Wong3; Yun Wah Lam4; Kelvin WK Yeung3; Huiru Tang1; Yunlan Wang1; 1Wuhan Institute of Physics and Mathematics, Wuhan, P. R. China; 2Third Military Medical University, Chongqin, P. R. China; 3The University of

Hong Kong Medical Centre, Hong Kong, China; 4City University of Hong Kong, Hong Kong, China

To investigate the effect of transgenic EGFP expression in vivo, we analyzed the metabonome of EGFP transgenic mice with an NMR-based metabonomic method. We found that the metabolic profiles of urine, liver and kidney were different in the EGFP transgenic mice compared to their wild type counterpart. The EGFP transgenic expression induced metabolic alternations: gluconeogenesis and transamination were being produced in the liver; there were metabolic disturbance of pyrimidine and amino acids, manifested by increased 3-ureidopropionate and decreased phenylacetate in the urine; Ethanolamine acts as the component of the membrane and TMAO as an osmolyte, both decreased in the kidney. These findings indicated that the function of the kidney was disturbed in some degree in response to transgenic EGFP.

Poster 251

A Simple Method to Remove Complex Background Signals from the 1H NMR Spectra of Mixtures

Nagana Gowda; Purdue University, West Lafayette, IN 1H NMR spectra of blood serum/plasma and diabetic urine contain strong background peaks due to the high concentrations of glucose, which make the underlying signals from other metabolites invisible. We present a simple background subtraction method, “Add to Subtract,” and show that it can reduce the glucose signals by 98% to allow retrieval of the hidden information. This procedure includes acquisition of a second spectrum with added glucose solution. The glucose-free spectra are then generated by spectral subtraction and used to identify biomarker candidate using multivariate statistical analysis. The principle of this approach is generally applicable for all quantitative spectral data and



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should find utility in a variety of NMR-based mixture analyses as well as in metabolite profiling.

Poster 252

Application of 2D selective-TOCSY HMBC for Structure Elucidation of Isomers in Mixtures without Separation

Tsang-Lin Hwang; Bo Shen; Mike Ronk; Maria Victoria Silva Elipe; Jacqueline E. Milne; AMGEN, Inc.,

Thousand Oaks, CA In the pharmaceutical industry, we are interested in the structure elucidation of impurities at levels greater than 0.1 % in the active pharmaceutical ingredient. One source for impurity generation is from isomers in starting materials. Proton peaks belonging to different isomers could be potentially identified in the 1D 1H NMR, when evaluated in combination with 2D COSY and HSQC data. However, in 2D HMBC data, correlation responses from different isomers may overlap, causing uncertainty of carbon assignments. This observation prompts us to design the 2D selective-TOCSY HMBC experiment to distinguish responses from different isomers in mixtures in order to obtain 2D NMR data for each isomer, thus eliminating the chromatographic isolation step to obtain material for NMR analysis.

Poster 253

Metabolite Identification in Biofluids Combining 2D LC and Isotope Resolved NMR

Fariba Tayyari; Purdue University, West Lafayette, IN The use of isotope tagging, in which molecules with various functional groups are chemically tagged with labeled derivatizing agents followed by detection by 2D NMR provides a powerful method for resolving complex samples. This approach allowed detection of over 100 metabolites in a single experiment with improved resolution and reproducibility. However, there are still many NMR detectable metabolites in biofluids that remain unknown. We present a new approach based on two-dimensional hydrophilic interaction chromatography to facilitate the resolution of these polar “tagged” metabolites in human serum and urine. The ability to separate structurally identical compounds chromatographically has resulted in the assignment of 12 and 15 metabolites in addition to the 21 and 23 previously identified in serum and urine, respectively.

Poster 254

Comprehensive Analysis of Coffee Bean Extracts by NMR Spectroscopy

Feifei Wei; Kazuo Furihata; Takuya Miyakawa; Masanori Koda; Fangyu Hu; Masaru Tanokura; The University of Tokyo,

Tokyo, Japan NMR-based metabolomics has been applied in food science. We present the comprehensive analysis of coffee bean extracts using detailed NMR assignment information for the application to the quality control of coffee. Metabolic components of green and roasted coffee bean extracts were comprehensively assigned in the complex mixture using various two-dimensional NMR spectra. The qualitative, quantitative and state analyses of their components were accomplished non-destructively on the basis of signal assignments. Furthermore, NMR spectroscopy coupled with multivariate analysis revealed the chemical changes during roasting process and the discrimination of coffee beans according to their species and origins. This comprehensive

NMR analysis provides an holistic insight of coffee beans and significant chemical markers to control the quality of coffee beans.

MOTION & DYNAMICS, 255 - 257

Poster 255

Investigating Conserved Motions in Pin1 Kimberly Wilson; Jill Bouchard; Xingsheng Wang; Jeffrey

Peng; University of Notre Dame, Notre Dame, IN Human Pin1 catalyzes phosphorylated Ser/Thr-Pro segments in several mitotic proteins. Residues displaying a change in side-chain flexibility upon substrate binding are highly conserved and highly correlated as identified through bioinformatic and correlation-based techniques. We present here initial dynamic analyses of backbone and methyl-bearing side chain residues on the conserved M130A and non-conserved I28A mutant Pin1 proteins. Measurements focus on similarities and differences compared to wild-type Pin1.

Poster 256

Modeling a System with Intrinsic Disorder: An NMR/MD Study of peptide-protein Encounter Complex

Tairan Yuwen; Yi Xue; Nikolai R. Skrynnikov; Purdue University, West Lafayette, IN

In this study we seek to characterize structure/dynamics of electrostatic encounter complex formed by intrinsically disordered protein (proline-rich Sos peptide) and its folded target (c-Crk N-SH3 domain). By introducing two point mutations in the hydrophobic grooves of the SH3 domain we disrupt the tight binding and shift the equilibrium toward the fluxional state which is underpinned by electrostatic contacts. This engineered state, which approximates the electrostatic encounter complex, is studied through 15N relaxation and chemical shifts. To construct an in silico model, we recorded a number of ~1 μs MD trajectories of the Sos-SH3 complex; these data are used as a source pool to form an ‘ensemble of MD trajectories’, which is tailored to reproduce the experimental NMR data.

Poster 257

Diacylglycerol Affinity and Binding Loop Dynamics in PKCδ C1B Domain

Mikaela Stewart; Tatyana Igumenova; Dept of Biochemistry and Biophysics, Texas A&M Uni, College Station, TX

Diacylglycerol sensitive Protein Kinase C (PKC) isoforms are activated when one or both C1 domains associate with diacylglycerol containing membranes. To investigate the mechanism behind varying diacylglycerol affinities of C1 domains, we carried out solution NMR experiments using PKCδ C1B domain and its diagnostic mutant, W123Y. The mutation decreases the diacylglycerol affinity more than one order of magnitude, but does not have a significant effect on the C1B structure nor sub-nanosecond dynamics. However, the apo mutant has a significant decrease in conformational dynamics of the ligand binding loops. Previously, we discovered the opposite trend in PKCα and Y123W mutant. Together with our previous findings, the data point to a link between conformational dynamics and C1 domain diacylglycerol affinity.



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MRI, 258 - 261

Poster 258 The Role of Nonlinear Gradients in Parallel Imaging: A K-

space Based Analysis Gigi Galiana1; Jason Stockmann1, 2; Leo Tam1; Todd

Constable1; 1Yale University, New Haven, CT; 2Harvard-MGH, Boston, MA

Sequences that encode the spatial information of an object using nonlinear gradient fields are a new frontier in MRI, with potential to provide lower peripheral nerve stimulation, windowed fields of view, curved slices that mirror physiological geometry, and very fast parallel imaging with multichannel coils. The acceleration for multichannel images is generally explained by the fact that curvilinear gradient isocontours better complement the azimuthal spatial encoding provided by typical receiver arrays. However, the details of this complementarity have been more difficult to quantify. We present a simple and intuitive framework for describing the mechanics of image formation with nonlinear gradients, and we use this framework to review some the main classes of nonlinear encoding schemes.

Poster 259

Optimal Control Excitation Contrast for Separation between Fast and Slow sodium

Fei Han; Jae-Seung Lee; Alexej Jerschow; New York University, New York, NY

With the availability of high-field MRI scanners, the 23Na MRI images become a promising tool for diagnosing diseases and for assessing the intra- vs. extracellular sodium balance. The sodium ions bound to tissues and organs may be subjected to slow motion with the quadrupolar relaxation as their dominant mechanism. In previous work, shaped pulses were developed to distinguish the slow-motion sodium ions from the fast-motion (free) ones, based on optimal control theory. However, these pulses require an additional high-power reading pulse and phase cycling, which may not be practical in a clinical setting due to power deposition limitations. Here, we present pulses optimized for directly maximizing the transverse signal from the bound sodium ions while suppressing that from free ones.

Poster 260

Simulations of Multi-Shot Spiral Imaging with Off-Resonance Correction and Variable Density k-Space

Sampling Gerald Matson1, 2; Hui Liu1, 3; 1Center for Imaging of

Neurodegenerative Diseases, San Francisco, CA; 2University of California, San Francisco, CA; 3NCIRE, San Francisco, CA Although spiral imaging has many potential advantages, including reduced acquisition time and suppression of flow and motion artifacts, the computational effort required for image reconstruction with correction of resonance offset effects has hindered its use. In this work, we show that the efficient algorithm that includes correction of resonance offsets recently introduced by Meng and Lei (MRM 63, 1691, 2010) can be applied to variable density spirals that under-sample the outer regions of k-space. Programs for generation of suitable spiral k-space sampling, and for reconstruction of simulated spiral k-space data, are discussed. The image reconstruction results from simulated data indicate that the Meng and Lei approach can provide efficient, high fidelity

image reconstruction even from under-sampled spiral k-space data.

Poster 261

Miniature 1.5 Tesla Cryogen Free MRI Magnets Jeremy Good; Jonathan Cole; Cryogenic Ltd, London, UK

Two miniature MRI magnets have been built that require no liquid helium and can be used anywhere electrical power is available. One unit is 1-5 Tesla 260mm bore and uses a three phase 2.5 watt compressor to provide cooling of the magnet. The homogeneity is a 5ppm over 120mm. The second is a 1 Tesla 150mm bore magnet that uses a 1 kilowatt single phase compressor, this has an 80mm homogenous volume. They can be used anywhere in the world and an MRI console with software is available to give a complete MRI system for laboratory studies. We plan to build 4 and 7 Tesla versions of these magnets shortly.

NMR & CRYSTALLOGRAPHY, 262 - 268

Poster 262

Coordination Chemistry and Solution Structure of Fe(II)-Peplomycin. Two Possible Coodination Geometries

Yang Li; university of wyoming, Laramie, WY The glycopeptide-antibiotic peplomycin is more effective in the treatment of certain cancers, and has less pulmonary toxicity. The solution structure of Fe(II)-peplomycin was determined from NMR data. We found that the coordination sphere of the metal is composed of the primary and secondary amines in β-aminoalanine, the pyrimidine and imidazole rings in the pyrimidinylpropionamide, the β-hydroxyhistidine moieties, the amine nitrogen in β-hydroxyhistidine, and either the carbamoyl group in mannose or a solvent molecule. The two coordination geometries have been tested against the NMR data indicating that both geometries are equally likely in solution for this compound in the absence of DNA.

Poster 263

Structural Basis for Ca2+-induced Activation and Dimerization of Estrogen Receptor Alpha by Calmodulin

Yonghong Zhang; James B. Ames; UC Davis, Davis, CA The estrogen receptor alpha (ER-a) regulates expression of target genes implicated in development, metabolism, and breast cancer. Calcium-dependent regulation of ER-a is critical for activating gene expression and is controlled by calmodulin (CaM). We present the NMR structures for the two lobes of CaM each bound to a localized region of ER-a (residues 287-305), and construct a model of the complete CaM/ER-a complex by combining these 2 structures with additional data. The two lobes of CaM both compete for binding at the same site on ER-a, which explains why full-length CaM binds two ER-a molecules and stabilizes ER-a dimerization. CaM facilitates ER-a dimerization without estrogen, and ER-a stimulation by either Ca2+ and/or estrogen may serve to regulate transcription in a combinatorial fashion.

Poster 264

NMR Studies on Various Cationic Natural Zeolite Natrolite with a Complete Degree of Si-Al Order in Hydrated and

Dehydrated States Aurélie Vicente; LCS - Université de CAEN, Caen, France



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Natrolite is one of the first natural zeolites, which have been reported in the literature by the early 1800’s. Its crystal structure has been established early on by 1930’s by Pauling and Taylor. Nonetheless, its unique chemical and structural characteristics have continued to be discovered up to date, probably due to the flexible connectivity of the NAT topology. Pressure and temperature have been shown to alter the structure and the composition. The aim of the present work is to gain detailed insights into the non-equivalent tetrahedral sites (T-sites) in hydrated and dehydrated forms of various extra-framework cation-exchanged natural natrolite to better understand the performance of these materials. Characterization mainly involve XRD techniques and advanced high resolution and correlation NMR experiments.

Poster 265

Solution NMR and Biophysical Analysis of the Cataract-associated R76S Mutant of Human γD-crystallin Fangling Ji; University of Pittsburgh, Pittsburgh, PA

We expressed the R76S γD-crystallin protein, a recently discovered mutation correlated with childhood-cataract in an Indian family, in E. coli and characterized it by CD and fluorescence spectroscopy, as well as determined its thermodynamic stability with respect to thermal/chemical denaturation. Surprisingly, no significant biochemical/biophysical differences were observed compared to the wild type, except a lowered pI. NMR assessment of its solution structure by RDCs and motional properties by relaxation measurements revealed no significant changes from wild type. In addition, kinetic unfolding/refolding experiments for R76S exhibited a similar degree of off-pathway aggregation suppression by αB-crystallin as wild type. Our overall results suggest that neither structural nor stability changes in the protein are responsible for the R76S γD-crystallin variant’s association with cataract.

Poster 266

Solid State NMR Evidence for Cross-Beta Assembly of Gas Vesicles

Marvin J. Bayro2; Eugenio Daviso1; Marina Belenky1; Robert Griffin2; Judith Herzfeld1; 1Department of Chemistry, Brandeis University, Waltham, MA; 2Francis Bitter Magnet Laboratory,

MIT, Cambridge, MA Functional amyloids have been identified in a wide range of organisms, taking on a variety of biological roles, and being controlled by remarkable mechanisms of directed assembly. Here we report that amyloid fibrils constitute the ribs of the buoyancy organelles of Anabaena flos-aquae. The walls of these gas-filled vesicles are known to comprise a single protein, GvpA, arranged in a low-pitch helix. Using MAS NMR correlation spectroscopy, we find detailed evidence for an extended cross-β structure. This amyloid assembly helps to account for the strength and amphiphilic properties of the vesicle wall. Buoyancy organelles thus dramatically extend the scope of known functional amyloids.

Poster 267

Solid-state NMR Structural Studies of an Amphiphilic n-type Nanotube

Subhradip Paul; PostDoctoral Researcher, Columbus, OH We present the structural studies of one-dimensional n-type organic nanotubes, which have been shown to facilitate rapid energy migration and are currently being explored for potential

applications as components of light-harvesting devices. 1D and 2D magic-angle spinning (MAS) solid-state NMR were utilized to perform the initial characterization of nanotubes containing uniformly 13C, 15N-labeled lysine head-groups which gave us the full resonance assignments of the lysines. Here we extend these initial NMR studies, with the ultimate goal of deriving a high-resolution structural model for the nanotubes that can aid in understanding their excited state characteristics. The studies gave us intermolecular distances for the lysine groups. We also probed intermolecular 13C-15N contacts using samples formed from a mixture of 13C- and 15N-labeled monomers.

Poster 268

High-Resolution Crystal Structure Elucidation of Inorganic Solids: Powder NMR Crystallography or

Synchrotron Diffraction Crystallography? Charlotte Martineau1; Boris Bouchevreau1; Frank Engelke2;

Julien Trebosc3; Olivier Lafon3; Jean Paul Amoureux3; Francis Taulelle1; 1Institut Lavoisier de Versailles (ILV), Versailles, France; 2Bruker Biospin, Rheinstetten, Germany; 3UCCS-CNRS UMR8181-Univ Lille1, Villeneuve D'ascq Cedex,

France Despite great improvements in diffraction techniques, structure resolution of hybrid materials from powder diffraction data remains challenging. Provided sufficient spectral resolution, NMR Crystallography can overcome the current limits of powder diffraction. We present two recent NMR Crystallography studies, where improved NMR resolution was critical to get model with structural resolution much higher than what is currently obtained from synchrotron measurements. First, a four-channel 2.5 mm CPMAS probe has provided in a fluorinated aluminophosphate NMR spectra with increased resolution, the key to describe the distribution of the fluorine atoms. Second, a new NMR experiment that permitted observation of 31P-27Al proximities at high-field with high-resolution in the quadrupolar dimension in aluminophosphate AlPO-DAE, has allowed solving its structure, which was impossible with diffraction.

NMR IMAGING: ADVANCES, 269 - 270

Poster 269

Design of Relaxation Selective Pulses using Optimal Control Theory

Alex Burum; University of Miami, Coral Gables, FL In this work, we apply optimal control theory to generate T2-selective pulses (pulses that null magnetization for a set of T2 values) that were robust to both B0 and B1 inhomogeneity and were compensated for T1 relaxation. The performance of the pulses were determined by measuring the magnetization profiles as a function of T2 on H2O samples with varying concentrations of paramagnetic species [MnCl2], and good selectivity close to the theoretical ideal magnetization was found.

Poster 270 Isolating CEST from MT Asymmetry by Simultaneous

Two-frequency RF Irradiation Jae-Seung Lee1, 2; Ravinder Regatte2; Alexej Jerschow1;

1New York University, New York, NY; 2NYU Langone Medical Center, New York, NY

Chemical exchange saturation transfer (CEST) and magnetization transfer (MT) contrast have enjoyed wide



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popularity recently in MRI applications. It is often difficult to separate genuine CEST signatures from MT effects, which are asymmetric with respect to the water resonance. We recently developed a method that utilizes simultaneous two-frequency rf irradiation, which can make MT effects independent of irradiation frequencies over a wide range, and thus can flatten out MT asymmetry. Based on the results from the simulations as well as experiments, we propose a new strategy to isolate CEST contrast from MT asymmetry contrast by using the two-frequency rf irradiation technique.

RESOLUTION & SENSITIVITY, 271 - 272

Poster 271 Self-resonant, Implantable, Radio Frequency Circuits for

in vivo Magnetic Resonance (MR) Imaging & Spectroscopy

Barjor Gimi1; Samuel Grant2; Richard Magin3; 1Dartmouth Medical School, Lebanon, NH; 2The Florida State University, Tallahassee, FL; 3University of Illinois at Chicago, Chicago, IL The miniaturization of radio frequency resonators provides increased signal-to-noise ratio (SNR) per unit volume in MR. The implanted microresonators then can operate in an entirely wireless mode, which provides ease of use and eliminates the risk of infection associated with implants with invasive, connecting wires. We outline the design, fabrication, characterization and testing of such wireless microresonators. We successfully demonstrated increased sensitivity in signal detection using a self-resonant microresonator. We are in the process of extending our studies to demonstrate in vivo imaging of small implanted cellular clusters using these implantable microresonators.

Poster 272

Phase Incremented Echo Train Acquisition (PIETA) Jay H Baltisberger2; Brennan Walder1; Eric Keeler1; Derrick Kaseman1; Kevin Sanders1; Philip J. Grandinetti1; 1The Ohio State University, Columbus, OH; 2Berea College, Berea, KY

We present an Echo Train Acquisition (ETA) approach where using CPMG is complicated or impossible. Adding ETA to multidimensional experiments creates an additional dimension for the echo count. In PIETA, the phase of the mixing pulse and every other refocusing pulse is incremented as one variable, creating yet another dimension. Fourier transform of the signal with respect to the PIETA phase converts the φ dimension into a δp dimension where desired and undesired pathway signals are separated. Unlike conventional phase cycling, PIETA doesn’t use a receiver phase master equation and facilitates simultaneous acquisition of multiple signal pathways. Unlike CPMG, PIETA can be appended to experiments with phase-modulated signals after the mixing pulse, and can be used to measure J-couplings.

SCREENING, 273 - 274

Poster 273

Absolute Shielding Scale for Multinuclear Magnetic Resonance Spectra

Karol Jackowski1; Michal Jaszunski2; Wlodzimierz Makulski1; Marcin Wilczek1; Piotr Garbacz1; Andrej Antusek3; 1University

of Warsaw, Warszawa, Poland; 2Institute of Organic Chemistry PAN, Warsaw, Poland; 3Slovak University of

Technology in Bratislava, Trnava, Slovak Republik

The method of shielding measurements available on a standard NMR spectrometer is demonstrated. It is based on the calculation of magnetic shielding in an isolated helium-3 atom and our investigation of resonance frequencies in the gas phase. Next the vantage point of the absolute shielding scale is transferred from helium-3 to another reference standard, such as a deuterated lock solvent, and one can conveniently use it in practice. The shielding constants can be determined this way for 1H, 2H, 13C, 15N, 17O and some other nuclei. As shown the chemical shifts can be entirely replaced by the parameters of shielding. The new method also allows the measurement of the first order isotope effect in shielding, what was never available before.

Poster 274

Automated Analysis of Niacin in Dietary Supplement Tablets by 1H NMR Spectroscopy

Sarah Luchsinger1; Kimberly L. Colson1; Michelle Markus1; Christian Fischer2; Mark Garvey2; Marc Wolff2; 1Bruker

BioSpin US, Billerica, MA; 2Bruker BioSpin GmbH, Rheinstetten, Germany

Niacin (B3) is a water soluble B-group vitamin, which is proven to help lower cholesterol. Here, a robust analytical method is presented that analyzes niacin within dietary supplement tablets by 1H NMR in full automation. Methodology was performed using the Assure-Raw Material Screening (RMS) software. The automated analysis involves 1.) identification of niacin through a spectral match, and 2.) absolute quantification using the principles of the PULCON1 method. Integration algorithm was optimized through a peak integration method, which took into consideration complex coupling patterns. The analysis generates a report summary, thus eliminating the need for manual spectral interpretation. This method was successfully tested on multiple supplement tablets. A simultaneous analysis of all B-group vitamins is being currently being developed.

SMALL MOLECULES & DRUG DISCOVERY, 275 - 298

Poster 275

Segmented Flow into Conventional 3 mm NMR Flow Probes Doubles Mass Sensitivity, Increases Automation Throughput

Roger Kautz; Barnett Institute of Chem and Biol Analysis, Boston, MA

Flow injection NMR (FIA-NMR) has proven valuable for acquisition of spectra directly from vials or plates, avoiding the time, expense, and automation for handling samples in tubes. Extending previous work in segmented flow (SFA) loading of microprobes, we show SFA loading avoids problems of conventional 3mm (60 uL) flow-NMR which derive from sample dispersion: sample dilution, concentration gradients, and carryover. SFA into a 60 uL cryo-flow cell was explored with minor changes to a commercial FIA platform (Protasis One-Minute NMR). A 60 uL sample loaded by SFA was seen to have twice the S/N as optimized FIA loading, better lineshape sooner after injection, faster clearing between samples, and a defined concentration (100%) which is valuable for ligand binding or qNMR.

Poster 276

NMR Investigations of the Prismylate Derivative(s) Obtained from Enzymatic Reactions



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Ilker Ün1; Neslihan Bozkurt1; Fatih Demirci2; Ayhan Çelik1; 1Gebze Institute of Technology, Gebze, Turkey; 2Anadolu

University, Eskişehir, Turkey Prismylate (4-Methyl-8-methylenetricyclo[3.3.1.(3,7)]decan-2-yl acetate) and its derivatives are important group of compounds which are utilized in both cosmetic; including decorative cosmetics, fine fragrances, shampoos, toilet soaps and non cosmetic products; including household cleaners and detergents. Its worldwide use is in the region of 0.1 metric tonnes per annum and mounting rapidly [1]. In this work, we have investigated enzymatic biotransformation of prismylate to its corresponding epoxide with high regio- and enantioselectivity. The resulting product(s) have been investigated by NMR. References: [1] S.P. Bhatia et al. / Food and Chemical Toxicology 46 (2008) S74–S78

Poster 277

Spectroscopic Analysis and Anti-diabetic Activity of a Polyherbal Formulation: NMR and LIBS Based Studies

Prashant Kumar Rai1; Gaurav Sharma1; Somenath Ghatak1; Geeta Watal2; Awadhesh K Rai3; Rama Jayasundar1; 1Dept

of NMR,All India Institute of Medical Science, New Delhi, India; 2Department of Chemistry, University of Allahabad, Allahabad, India; 3Department of Physics, University of

Allahabad, Allahabad, India The present paper reports, the NMR spectroscopy based chemical analysis of poly herbal formulation and laser induced break down spectroscopy (LIBS) based detection of trace minerals. Certain combination of metabolites and trace elements present in plants have anti diabetic properties and could be used as a promising therapeutic approach for the prevention and treatment of diabetes mellitus. The present work is an attempt to use NMR spectral data as fingerprinting for identifying major plant metabolites and correlating their presence with their pharmacological attributes. This is the first study of its type in which the role of metabolites and the trace mineral elements present in the plants, in management of glycemic profile using modern scientific tool such as NMR and LIBS.

Poster 278

Structure of a CXCL12: Inhibitor Complex and Fragment-Based Development of Molecules that Inhibit CXCR4-

Mediated Migration Joshua Ziarek; Medical College of Wisconsin, Milwaukee, WI

The CXCL12/CXCR4 chemokine interaction is a high-priority clinical target because of its involvement in multiple pathologies including autoimmune disease, cardiovascular disease and cancer. However, disrupting the large protein-protein interface has proven difficult for traditional drug discovery approaches, emphasizing the need for alternative strategies. Although chemokine ligands are generally viewed as “undruggable” proteins based on size, recent studies have identified small molecules that target the chemokine CXCL12. Here we report the first structure of a chemokine:inhibitor complex. Guided by this NMR structure, we used a fragment-based approach to evolve the initial hit to a class of molecules with greater affinity, efficiency, and the capability to block in vitro cell migration – a critical advancement in the rational development of inhibitors.

Poster 279 Characterization of Tranilast Binding to Amyloid-β: A Multidisciplinary Approach to Structural-Based Drug

Discovery for Intrinsically Disordered Proteins Chris Connors; David Rosenman; Angel Garcia; Chunyu

Wang; Rensselaer Polytechnic Institute, Troy, NY Alzheimer’s disease (AD) pathogenesis is likely caused by the aggregation of amyloid-beta (Aβ), an intrinsically disordered protein (IDP). There is no effective treatment of AD, making the identification of drug interactions with Aβ necessary for future treatments. Because Aβ samples many conformations, making experimental structure determination impossible, screening of compounds was accomplished using molecular docking of REMD simulated centroid structures to a small molecule database. Promising compounds were selected and chemical shift perturbation and STD experiments were used to determine binding in vitro. Aggregation assays were utilized to determine a compounds effect on Aβ aggregation. Tranilast is the first novel Aβ binder discovered using this approach, which may be applicable in the future to other disease-causing IDPs.

Poster 280 uHTS by NMR of Combinatorial Libraries: A Powerful

Fragment-based Approach to Ligand Discovery Bainan Wu; Sanford-Burnham Medical Research Institute, La

Jolla, CA In the past decade, fragment based ligand design (FBLD) approaches have become more widely used in drug discovery. Compared to high throughput screening (HTS), FBLD can detect fragments of weak binding and is less prone to artifacts. However, the challenge of FBLD is the evolution of weak fragments into more mature compounds. Here, we introduce a new fragment screening strategy, uHTS by NMR, which combines combinatorial chemistry and protein NMR spectroscopy to enable the screen of fragments pre-assembled on a common backbone. We first demonstrate the feasibility of the uHTS by NMR on a well-studied target, baculovirus IAP repeat 3 (BIR3) domain. Further, we report novel ligands obtained by the method that target EphA4 receptor.

Poster 281 Quantitative Determination of Low levels of Irbesartan

Form B in Avalide Tablets by ssNMR Spectroscopy George B. Crull; Shawn Yin; John Grosso; Duohai Pan;

Bristol-Myers Squibb, New Brunswick, NJ The cardiac drug, Avalide is a combination of an Irbesartan, and a Hydrochlorothiazide. Control of the polymorph in the tablet is important as each polymorph has differences in dissolution rate. A quantitative C-13 CPMAS ssNMR procedure was developed to measure the amount of each form of irbesartan in laboratory mixtures and commercial tablets. Peak position and line widths from an equal molar mixture were used in subsequent data analysis. The areas of three resonances from each polymorph were calculated by deconvolution, averaged and the ratio was determined. A LOD of 1% was determined for form B. The reproducibility, accuracy and precision were determined. This demonstrates the role and importance of ssNMR as a primary method, which enables development of secondary methods.



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Poster 282 Quantitation of Various Phases of Commercial Lactose

using Solid-state NMR Anuji Abraham; Denette Murphy; Duohai Pan; Daniel

McNamara; George B. Crull; Bristol-Myers Squibb, New Brunswick, NJ

Lactose is a disaccharide consisting of a galactose and a glucose unit. There are four reported forms of lactose, a-Lactose monohydrate, a-Lactose anhydrous, a-Lactose anhydrous and �b-Lactose. Lactose is widely used as a filler or filler-binder in the manufacture of pharmaceutical tablets and capsules. Understanding the phase purity of lactose is very important as drug stability, drug-lactose interaction and processability (especially compaction and flow) could be very dependent on various lactose phases present. The study aims to develop a robust technique to provide a complete characterization of lactose phases present in commercial lactose samples. Using the optimized C-13 CPMAS conditions, lactose from different vendors has been studied and the phases have been quantified, therefore giving insights into drug development.

Poster 283

Radiation Damping Based NMR Spectroscopy for Ligand Screening

Peng Sun1, 2; Bin Jiang1; Xu Zhang1; Maili Liu1; 1Wuhan Institute of Physics and Mathematics, CAS, Wuhan, China;

2Graduate School of Chinese Academy of Sciences, Beijing, China

Ligand based NMR techniques are important tools to probe ligand-biomolecule interactions, such as saturation transfer difference spectroscopy (STD), water ligand observed via gradient spectroscopy (waterLOGSY), and NOE pumping. A principal part of those NMR techniques is selective saturation or excitation of resonances of biomoleculer or water. Here we proposed a new method based on radiation damping, in which water selection was achieved by controlling the time to start the gradient for radiation damping destruction. The method is robust and sensitive to identify ligand of large biomolecules.

Poster 284

Structural Analysis of the PEGylation Chemistry of PEG-Interferon alfa-2a by NMR

Fabio Casagrande; F. Hoffmann-La Roche AG, Basel, Switzerland

The market for biopharmaceuticals is rapidly expanding as novel protein drugs show promise in treating a wide range of diseases. Similar to generic drugs that replace branded products, biosimilars hit the markets soon after the patents of biopharmaceuticals expire. However, in contrast to small molecules structural properties of these proteins drugs are difficult to analyze. In this work, the methodology is described to determine the PEGylation chemistry of protein drugs by high-resolution NMR techniques. The structural information of the PEGylation chemistry is essential for the comparison of biosimilars with their corresponding biologic brands that are still covered by valid patents. Thus, verification can be obtained whether new PEGylated protein drugs infringe existing patents or if expensive clinical studies are required.

Poster 285 13C T1 Spin-lattice Relaxation Studies for Atropisomerism

Identification of 4(1H)-Quinolones with Antimalarial Activity

Andrii Monastyrskyi; R. Matthew Cross; Edwin Rivera; Roman Manetsch; University of South Florida, Tampa, FL

The modern pharmaceutical industry is affected by chirality to a great extent: it is well known that stereoisomers may differ in biological activity, pharmacokinetics, and toxicity. Based on preliminary data, 3-aryl 4(1H)-quinolones with atropisomeric character possess improved in vivo antimalarial efficacy in P. berghei infected mouse model. These results suggest that only one of the potential atropisomers is biologically active. Herein we report temperature dependent kinetic NMR experiments for the determination of the rotational barrier of stable conformational isomers of 3-aryl 4(1H)-quinolones. Also relative flexibility of C-H vectors was monitored by 13C T1 spin-lattice relaxation experiments where shorter relaxation times are indicative of relatively slower segmental motion or flexibility.

Poster 286

The Automatic Generation of Alternative Chemical Structures for Concurrent NMR Verification

Sergey Golotvin1; Ryan R. Sasaki2; 1ACD Moscow, Moscow, Russian Federation; 2ACD/ Labs, Toronto, ON

A novel approach towards automated structure verification entitled, "Concurrent Verification" was reported previously1

which highlighted many advances in this area, particularly in the reduction of false positive results. This study focuses on a new method for automatically generating the alternative chemical structures required to make the concurrent verification approach reach practical application in synthetic chemistry and NMR workflows. An explanation of the methodology and logic used to create alternative chemical structures, as well as the overall performance of this system as it relates to false negatives and false positives will be presented. 1. Golotvin, S., Pol, R., Sasaki, R., and Nikitina, A. A New Approach Towards False Positive Reduction in Automated NMR Structure Verification, ENC 2011 Poster #386

Poster 287

NMR Spectroscopic Analysis and in-vitro Antioxidant Efficacy of the Medicinal Plant Tribulus Terrestris

Somenath Ghatak; All India Institute of Medical Sciences, New Delhi, India

The role of phytochemicals in disease prevention due to antioxidant potential is being studied extensively. In this study, aqueous extract of the aerial parts of the medicinal plant, Tribulus terrestris, has been studied using spectroscopy and also evaluated for its antioxidant potential. The latter was assessed using (DPPH), (FRAP), total phenolics, flavonoids and flavonols assays. The chemical profiling was done using NMR (700 MHz, Varian, USA) and trace element analysis was done using Laser-induced breakdown Spectroscopy (LIBS) (Ocean Optics 2000+, USA). NMR spectroscopic results showed common primary metabolites such as sugars and amino acids. It is, thus, interesting to note that the observation of the secondary metabolite in the NMR, Mg and Ca and high antioxidant potential are inline.



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Poster 288 More Accurate 1JCH Coupling Measurement in the

Presence of 3JHH Strong Coupling in Natural Abundance Bingwu Yu1; Hugo Van Ingen2; Vivekanandan Subramanian3; Christoph Rademacher4; Scott E. Norris5; Daron Freedberg1; 1CBER/FDA, Bethesda, MD; 2University of Toronto, Toronto,

ON; 3University of Michigan, Ann Arbor, MI; 4Max Planck Institute of Colloids and Interfaces, Berlin, Germany;

5FDA, Rockville, MD J couplings are used to calculate RDCs and deduce molecular structure. We report significant discrepancies of up to 7 Hz between 1JCH values measured with HSQC type pulse sequences in the 1H dimension from those measured in the 13C dimension. We demonstrate that these discrepancies arise from strong scalar coupling and are not a result of poor digital resolution. Product-operator formalism analysis confirms that line shape distortions result from irremovable antiphase terms and spectral simulations show that the apparent 1JCH measured with HSQC in either dimension can be in error by up to 4 Hz. Spectral simulations can reproduce the errors induced by strong coupling and that these can be used to extract true 1JCH values.

Poster 289

Inversion and Refocusing Pulses from Nonlinear Optimization

Douglas E. Brown; Indiana University, Bloomington, IN Broadband inversion and refocusing pulses as well as selective inversion pulses have been produced from nonlinear optimization. The optimization procedure uses all phase values for the shaped pulses as variables. The broadband pulses developed with this method achieve maximum adiabicity with bandwidths of 100 KHz to 200 KHz by maintaining a linear frequency sweep in the centers. These pulses compare well to BIP and BIPBOP pulses. Refocusing pulses were also produced from 90x pulses followed by their time and phase inverses. These are the widest bandwidth single refocusing pulses to date. Finally, selective inversion pulses using the same optimization procedure will also be presented.

Poster 290

Discovering HCV Polymerase Drugs, NMR Tools, and Interesting Chemical Properties

Steven Laplante; Boehringer Ingelheim (Canada) Ltd., Laval, Canada

NMR played an important role in discovering drugs that target the HCV polymerase. NMR was applied at many steps along the discovery pathway such as (1) triaging screening hits, (2) identifying the binding pocket of this multi-pocketed polymerase, (3) distinguishing between ligand segments that were solvent exposed versus those that contact pocket, (3) for determining ligand free versus bound conformation and dynamic properties, (4) metabolite ID, and more. The ensemble of NMR-based knowledge enabled the team to identify potent compounds and to “linker hop” to alternate series that resulted in launching of compounds to clinic. Interesting properties were also found such as compound self-aggregation and often overlooked conformation-based chirality. In conclusion, NMR has a promising future in the pharmaceutical industry.

Poster 291 Monitoring Acetylcholinesterase Inhibition by Oximes

and Hydrazones using NMR Jose Daniel Figueroa-Villar; Sibelle Soares; Gustavo Rocha;

Elaine Petronilho; Military Institute of Engineering, Rio De Janeiro, Brazil

The effect of neutral oximes and hydrazones on AChE was tested by 1H NMR, indicating some of these compounds as reasonable AChE inhibitors. The study of interaction of oximes and hydrazones with the active site of EeAChE was carried out by T1 and T2 relaxation times and their diffusion coefficients, with and without the presence of the enzyme, confirming their interaction with AChE. The results indicate that NMR is a better efficient method for monitoring the action of AChE than the Ellman test, showing that neutral oximes and cationic hydrazones display a significant AChE inhibition activity, with potential for treatment of Alzheimer disease and as defense agents against neurotoxic organophosphorus compounds.

Poster 292

Structure Elucidation of Xenobiotic Metabolites by NMR: A Pharmaceutical Perspective

George Doss; Merck, Rahway, NJ Mass spectrometry has been the method of first choice for the structure determination of metabolites of xenobiotics. NMR spectroscopy is commonly perceived as an insensitive method and thus usually employed at a much later stage, often for confirmation and/or elucidation of exact metabolites structures. Recent business pressures in the pharmaceutical industry has led to deferring NMR analysis until it is deemed absolutely necessary. This poster presents examples where NMR analysis has solved difficult metabolites structures that were elusive, unexpected, and/or inconsistent with the initially proposed structure. A variety of NMR methods were employed depending on the nature of the problem and the resources available at the time.

Poster 293

NMR Spectroscopic Characterization and Evaluation of Anticancer Potential of a Polyherbal Formulation on

HepG2 Cell Line Gaurav Sharma1; Rama Jayasundar2; Shyam S. Chauhan3;

Thirumurty Velpandian4; 1All India Institute of Medical Sciences (AIIMS), New Delhi, India; 2Dept of NMR, AIIMS, New Delhi, India; 3Dept of Biochemistry, AIIMS, New Delhi,

India; 4Dr R P Center of Ophthalmic Sciences, AIIMS, New Delhi, India

NMR is a versatile tool to characterize chemicals, biomolecules, metabolites etc. and is widely used to analyze drugs and herbal formulations. In this study, a polyherbal formulation (MK) used in the Indian indigenous system of medicine for the treatment for cancer is analyzed spectroscopically and also evaluated for its anticancer potential using MTT and AnnexinV-FITC PI apoptosis detection assays on liver cancer cell line (HepG2). In addition, its antioxidant potential has also been evaluated using FRAP assay. The proton 1D and 2D (TOCSY) spectra showed resonances from metabolites known to play crucial role in cancer cells. The formulation showed significant cytotoxicity and induces apoptosis in Hep G2 cancer cells as well as contains antioxidants.



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Poster 294 Weak Blocker to Plexin-B1/LARG “Hot-Spot” Delineated

by NMR Pseudocontact Shifts and Residual Dipolar Couplings

Ke Ruan; School of Life Science, University of Science and, Hefei, China

The blocker of protein LARG and Plexin-B1 complex has been serendipitously discovered when we measure the pseudocontact shifts introduced by lanthanide tag Ln(DPA) 3

3- to LARG PDZ domain. Dipicolinic acid (DPA) as a weak binder in the known protein-protein interaction “hot-spot” has been further confirmed by HSQC titration. We describe our progress in exploiting the spatial information of the weak binder with respect to LARG, retrieved from NMR pseudocontact shifts and residual dipolar couplings, as well as the structure-based discovery of new blockers as analogs of DPA.

Poster 295

Model-Free Solid-State NMR Solid Mixture Component Analysis using the Direct Exponential Curve Resolution

Algorithm Dirk Stueber; Merck & Co., Inc., Rahway, NJ

The present work presents the utilization of the direct exponential curve resolution algorithm (DECRA) in a model-free, quantitative component analysis of mixtures of pharmaceutical solids based on T1-modulated ssNMR data.

Poster 296

Proton-Fluorine Correlation using Unresolved J-couplings

Peter Howe; Syngenta, Bracknell, UK Fluorine containing compounds are rare in biological systems so fluorine NMR spectroscopy can detect and quantify fluorinated xenobiotics in crude biological extracts. The high sensitivity of fluorine NMR allows the detection of compounds containing isolated trifluoromethyl groups at nanogramme levels. However, it only provides limited structural information about trifluoromethyl containing compounds owing to the difficulty of interpreting fluorine chemical shifts, and because of the low sensitivity of HOESY experiments used to correlate fluorine nuclei with protons. This presentation demonstrates that long-range proton–fluorine couplings can be used to correlate protons with nearby trifluoromethyl groups with significantly higher sensitivity than HOESY. This can even give correlations when the proton-fluorine couplings are less than the observed fluorine resonance linewidth.

Poster 297

WYE-120318, a Ring Contraction Product of Methylnaltrexone -Structure Revision of Coniothyrione

Fangming Kong; Bao Nguyen; Pfizer, Groton, CT A contracted ring degradation product, WYE-120318 (2), was discovered during the analytical method development for methylnaltrexone bromide (1). The compound was isolated by HPLC fractionation, and its structure was determined by spectroscopic data analyses. WYE-120318 is formed through benzyl-benzilic acid type rearrangement reaction. The proposed structure and formation mechanism are confirmed by the synthesis of WYE-120318 from methylnaltrexone. Remisporine A (3) is the first reported naturally occurring cyclopentadiene compound. The structure of remisporine A was deduced from its dimer remsporine B (4). The discovery

of coniothyrione (5) supports the presence of remisporine skeleton in nature. However, the regional chemistry of the chloro-substituent in the coniothyrione structure needs to be revised based on NMR data and biogenesis analysis.

Poster 298

Structural Transitions of a Branched Antimicrobial Peptide in Heterogeneous Condensed Media

Yang Bai; School of Biological Science, Nanyang Technologica, Singapore, Singapore

Covalently branched antimicrobial peptides have been shown to have improved antimicrobial properties while retaining host biocompatibility. However, little is known about their molecular interactions with the bacterial cell walls and membranes. We examined the structure/activity relationships of a newly designed cationic, branched antimicrobial peptide using fluorescent probes, electron microscopy, MD simulations and high resolution NMR in solution and in condensed state to study the peptide reconstituted in gram negative bacterial outer and inner membrane mimicks. The results show that the peptide efficiently induces LPS structural phase transitions while maintaining high mobility within LPS assembly lattice. In lipid membranes, the peptide undergoes structural compaction strongly interacting with negatively charged lipids causing redistribution of the latter in the matrix of neutral lipids.

SOFTWARE & HARDWARE, 299 - 306

Poster 299

Fast Forward Maximum Entropy Reconstruction of One- to Multidimensional NMR Spectra

Nicholas Balsgart; Thomas Vosegaard; University of Aarhus, Aarhus, Denmark

Forward Maximum entropy (FM) was recently introduced by Hyberts et al. [Hyberts et al. JACS 129 (2007)] as a stable algorithm for reconstruction nonlinear sparse sampled datasets. Using the FM principle, we have developed a faster algorithm, Fast Forward Maximum entropy (FFM), which opens new possibilities for reconstruction of one- to multidimensional spectra. We demonstrate the method's ability to reconstruct sparse data in one and two dimensions and for up to 10 fold signal-to-noise improvements in one-dimensional spectra.

Poster 300

Computer-Assisted Structure Elucidation of Psychotripine with Incomplete NMR Information

Mikhail Elyashberg1; Ryan R. Sasaki2; 1ACD Moscow, Moscow, Russian Federation; 2ACD/Labs, Toronto, Canada

Psychotripine was reported as a new trimeric pyrroloindoline derivative from Psychotria pilifera[1]. It is a non-planar molecule with a formula weight of 514.633 that possesses an unprecedented carbon skeleton with 11 rings bearing a hexahydro-1,3,5-triazine unit. This molecule was the focus of a Computer-Assisted Structure Elucidation (CASE) study whereby only key correlations reported in the original publication were used for analysis. This study reveals how the software was able to generate and prefer the exotic and correct structure proposed by the original authors with limited and incomplete NMR information.



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[1] X.-N. Li, Y. Zhang, X.-H. Cai, T. Feng, Y. -P.Liu, Y. Li, J. Ren, H.-J. Zhu, and X. -D. Luo Organic Letters, ASAP, doi 10.1021/ol202536b

Poster 301

CONNJUR Workflow Builder: An Enhanced Actor Set for Spectral Reconstruction of NMR Data

Gerard Weatherby1; Colbert Sesanker2; Matthew Fenwick2; Jay Vyas2; Heidi J.C. Ellis1; Michael R. Gryk2; 1Western New England University, Springfield, MA; 2UCONN Health Center,

Farmington, CT The authors have previously presented a prototype of such an integrated, workbench environment, which we call CONNJUR Workflow Builder (CONNJUR-WB). In this poster we announce the distribution of an enhanced set of actors, providing support for a large portion of the processing functions provided by nmrPipe and the Rowland NMR Toolkit. CONNJUR is coded in Java to support the contributions of a wide range of developers and capitalizes on other open source software for its development (e.g. using MySQL as the relational database and CONNJUR-ST for spectrum translation). CONNJUR-WB is designed so that spectroscopists can code their own NMR data processing actors to further extend the actor set described in this poster.

Poster 302

An Expert System for the Automatic Assignment of 1H NMR Spectra of Small Molecules

Carlos Cobas1; Michael Bernstein1; Esther Vaz1; Felipe Seoane1; Maruxa Sordo1; Santi Dominguez1; Manuel Perez1;

Stanislav Sykora2; 1Mestrelab Research, Santiago De Compostela, Spain; 2Mestrelab/Extra Byte, Castano Primo,

Italy We present an integrated new software solution aimed at the automatic assignment of 1H NMR spectra of small molecules. It is based on an expert system constructed on principles of fuzzy logic with probabilistic methods used for the classification of the different resonances in the spectrum as well as for the enumeration of all the most likely assignments in the spectrum. The results obtained when the algorithm was applied to a large number of typical organic molecules of medium complexity and molecular mass show that more than 75% of all protons in the test set are successfully and correctly assigned. Finally, the system has been designed to take into account the possibility of incorporating additional NMR experiments (2D correlation spectra).

Poster 303

A Tool for Marking Chemical Shifts and Couplings on 1D and 2D Spectra in vnmrj

Ion Ghiviriga; University of Florida, Gainesville, FL This application does what a chemist would do with a pencil and a ruler on the spectra, but nicer and faster. Chemical shifts and couplings can be marked on the spectra using the cursors, then saved with the data, or written as an asscii file. Chemical shifts marked on a 1D spectrum can be retrieved on the 2D spectra. Alternately, one can mark chemical shifts on 2D spectra, in both dimensions, and then save them or write them to a file.

Poster 304 Automated QC with Compound Structure Verification and

Quantitation Michael Bernstein1; Carlos Cobas1; Felipe Seoane1; Stanislav

Sykora2; 1Mestrelab Research, Santiago De Compostela, Spain; 2Mesltrelab/Extra Byte, Castano Primo, Italy

We have developed a highly automated software system that automatically performs the following tests on NMR spectra of organic compounds in solution: purity, solvent impurities, concentration, structure confirmation (ASV), and assignments. 1H and 1H-13C HSQC spectra can be used alongside LC-MS and LC-UV data. The software can run in a batch mode, facilitating highly automated work-flows. We shall describe the operation and performance of the software, and some of the unique algorithms that make this very complex task possible.

Poster 305

Reaction Monitoring using NMR – Data Manipulation Solutions

Michael Bernstein; Carlos Cobas; Isaac Iglesius; Mestrelab Research, Santiago De Compostela, Spain

NMR has long been a preferred tool for the study of chemical reaction mechanism and kinetics because of the richness of the information that is reported in the data. However, th following may require further processing: •Excellent baseline correction •Peak alignment •Real time kinetic data analysis with instant analysis, reporting, and decision making Ee present a new software module that includes a number of sophisticated algorithms and capabilities that are applicable to Reaction Monitoring. The results confirm that NMR data are very useful in monitoring chemical reactions, and software procedures can be used to speed up the analysis and accommodate a number of spectroscopic and instrumental complications.

Poster 306

CLEAN Processing of Randomly Sampled Multi-Dimensional NMR Data

Jun Ashida2; Junichi Kurita2; Eriks Kupce1; 1Agilent Technologies, Oxford, UK; 2Agilent Technologies Inc., Tokyo,

Japan We show that the CLEAN processing that was introduced for reconstructing multidimensional spectra from projections is also useful for processing randomly sampled data sets. The technique was tested using randomly sampled 2D and 3D liquids and solids spectra. The time saving factor of 5 to 6 was achieved in 2D applications while in 3D experiments a factor of 20 to 30 is readily achievable. We show examples of applications to bio-molecules and small organic molecules, both in liquids and in solid state. The techniques is applied to a variety of experiments, such as routine 3D protein backbone assignment experiments, two-dimensional HSQC, HMBC, DQ-COSY, TOCSY as well as multi-receiver experiments.



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SOLIDS: BIO-APPLICATIONS, 307 - 337

Poster 307 NMR Studies of the Effect of SP-B1-25 on Lipid Dynamics

in Natural and Synthetic Lung Surfactant Lipid Preparations

Joanna R. Long; Suzanne Farver; Adam Smith; University of Florida, Gainesville, FL

Lung surfactant (LS) is a lipid-rich substance that minimizes surface tension in the alveoli. Surfactant protein B (SP-B) is critical to formation of a stable lipid layer at the air/water interface. SP-B1-25 has shown particular promise as a substitute for SP-B in LS replacement therapy. We will present 2H and 31P solid-state NMR studies which elucidate the function of SP-B1-25. We will describe the behavior of individual lipids in native calf lung surfactant extract (CLSE) and the effect of SP-B1-25 on lipid behavior in therapeutic CLSE and synthetic lipid mixtures based on the composition of CLSE. A highlight of these studies is the specific effect SP-B1-25 has on DPPC dynamics in all the lipid preparations characterized.

Poster 308

Solid-State NMR Investigation of the Structure of Membrane-Bound Fusion Peptide of Parainfluenza Virus 5

Hongwei Yao; Tuo Wang; Mei Hong; Department of Chemistry, Ames, IA

The membrane-bound structure of the fusion peptide (FP) of the parainfluenza virus 5 (PIV5) is investigated usingsolid-state NMR to elucidate the structural basis of viral membranes fusion. 13C chemical shifts of site-specifically labeledPIV5 FP in DMPC bilayers were measured using 1D and 2D 13C correlation experiments. These chemical shifts indicate aslow conformational change of the peptide in the membrane. The dynamics and membrane topology of the equilibriumstructure were investigated using 2D dipolar coupling and intermolecular spin diffusion experiments, while the lipidinteractions of the PIV5 fusion peptide were probed using 31P and 2H NMR. These results give fresh insights into how classI fusion peptides cause viral-host membrane fusion.

Poster 309

Structural Changes of Bovine Cortical Bone after Compressive Loading Revealed by Solid State NMR

Peizhi Zhu; University of Michigan, Ann Arbor, MI The effect of applied load on bone at the ultrastructural and molecular levels remain incompletely understood. It is still not known exactly how collagen fibrils and mineral crystallites deform to mechanical load in either the elastic or plastic deformation regimes. In this study, we use 1H and 31P solid state NMR to study chemical structure changes of bone mineral when tissue specimens are mechanically loaded. 31P NMR spectra show mineral ion spacing changes even under loads in the low mega-Pascal range. Thus bone mineral can no longer be considered as a completely rigid contributor to the viscoelastic behavior of bone, let alone to the plastic distortion.

Poster 310

Antiparallel β-Amyloid Fibril Formed by a Mutant of β-Amyloid Peptide Associated with Familial Alzheimer’s

Disease

Wei Qiang; Robert Tycko; National Institutes of Health, Bethesda, MD

Structure of β-amyloid (Aβ) fibril is closely related to its toxicity to neurons, and therefore is important to the elucidation of pathological mechanism of Alzheimer’s disease (AD). I will describe an experimental protocol which captured a metastable, cytotoxic intermediate fibril formed by the Iowa mutant Aβ peptides. Using solid state NMR spectroscopy and electron microscopy, we identified that the intermediate fibril contained an antiparallel β sheet hydrophobic core which has not been reported previously for Aβ fibrils formed by 40 or 42-residue peptides.

Poster 311

First Steps of an In Cell Solid-State NMR Study of Membrane Proteins in Proliferating Bacteria

Dror E. Warschawski1; Xavier Warnet1; Oana Ilioaia1; Eric Guittet2; Bruno Miroux1; 1CNRS / Université Paris Diderot,

Paris, France; 2CNRS, Gif-sur-Yvette, France We wish to study membrane proteins inside the cells where they are produced, using special proliferating bacterial strains. We have obtained preliminary data on the lipid composition and topology of such bacteria, from lipid 31P resonances. Solid-state NMR of intact bacterial cell pellet or isolated intact bacterial membranes may be a method of choice to follow the kinetics of membrane assembly, the production of cardiolipids and the formation of combs. Energetics parameters such as ATP/ADP ratio may also be obtained using 31P NMR. Uniformly or specifically 13C and 15N labeled samples can also be produced, in order to get new insight about protein folding directly inside the cells.

Poster 312

Band-Selective Homonuclear Decoupling during 13C Acquisition for Solid-State Proteins

Chen Yang1; Jochem Struppe2; Leonard J Mueller1; 1University of California, Riverside, Riverside, CA; 2Bruker-

Biospin, Billerica, MA Advances in sample preparation, hardware design, and pulse-sequence methodologies have progressed to the point where it is common in solid-state NMR spectroscopy to resolve J-couplings between 13C nuclei in U-13C,15N-labeled proteins. In many cases, J-coupling interactions are now the dominant source of inhomogeneous broadening. Here, we present a general method for band-selective homonuclear decoupling capable of removing the J-coupling interaction between Ca and C' spins during direct 13C acquisition. This windowed approach introduces negligible (~300ms) pulse breaks into much larger (>4ms) sampling windows to efficiently refocus the J-coupling interaction during detection and can be appended to any existing correlation method that detects 13C. We find increased resolution and sensitivity as illustrated here for CACO, NCO, and NCA correlation.

Poster 313

Revealing Protein Structures in Solid-phase Peptide Synthesis by 13C Sold-state NMR: Evidence of Excessive

Misfolding for Alzheimer’s β Songlin Wang; Yoshitaka Ishii; Univ. Illinois at Chicago,

Chicago, IL Solid-phase peptide synthesis (SPPS) is a widely used technique in biology and chemistry.



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However, the synthesis yield in SPPS often drops drastically for longer sequences, presumably due to the occurrence of incomplete coupling reactions. The underlying causes for this problem are hypothesized to be a sequence-dependent propensity to form secondary structures. However, few methods are available to study the site-specific structure of proteins or long peptides that are anchored to the solid support used in SPPS. This study presents a novel solid-state NMR approach to examine protein structure in the course of SPPS for the 40-residue Alzheimer’s β-amyloid (Aβ) as a useful benchmark. This approach is likely to be applicable to a wide range of peptides/proteins synthesized through SPPS.

Poster 314

Determining Lateral Diffusion Coefficients of Bilayer Lipids via 31P CODEX

Qasim Saleem1, 2; Angel Lai1, 2; Peter Macdonald1, 2; 1University of Toronto Mississauga, Mississauga, Canada;

2University of Toronto, Toronto, Canada Lateral diffusion of lipids in biological membranes is essential to their function. 31P CODEX (Center band Only Detection of Exchange) was utilized to measure lateral diffusion coefficients of phospholipids in large unilamellar bilayer vesicles. Knowledge of vesicle size and size distributions, as determined via dynamic light scattering, and solution viscosity, as determined via pulsed field gradient NMR, permitted a separation of vesicle tumbling and lateral diffusion contributions to the observed correlation time. In this fashion, lateral diffusion of different phospholipids was monitored simultaneously. We anticipate that this approach to measuring phospholipid lateral diffusion will prove particularly useful in cases of heterogeneous phospholipid mixtures, and/or heterogeneous phase distributions, such as those induced by various membrane-associating proteins.

Poster 315

Protein-Protein Interactions in the Bacterial Replisome Studied by Solid-State NMR

Stefan Jehle1; Michele Felletti1; Yao Wang2; Claire Mason2; Torsten Herrmann1; Lyndon Emsley1; Nicholas E. Dixon2; Anne Lesage1; Guido Pintacuda1; Alessandro Marchetti1; 1Center for NMR at Very High Fields - ENS/CNRS Lyon, Villeurbanne, France; 2School of Chemistry, University of

Wollongong, Wollongong, NSW, Australia In the bacterial DNA replication machinery (replisome), the single-stranded DNA-binding protein (SSB) binds to ssDNA to protect it from reannealing and degradation. More importantly, however, SSB plays key roles in DNA replication, recombination and repair, where it recruits many DNA processing enzymes by tethering them through its conserved C-terminal protein-protein interaction motif (SSB-Ct). Here we show that the application of solid-state NMR at very high fields (1GHz) provides, for the first time, residue-specific information for the interaction of SSB-Ct with its own SSB DNA-binding domain. This interaction acts as a switch that directs recruitment of secondary binding proteins specifically to ssDNA-bound SSB. This work clearly demonstrates the potential of high-resolution ssNMR for the characterization of large dynamic protein complexes.

Poster 316

The Janus Face of α-synuclein

Julia Gath1; Birgit Habenstein1, 2; Beat Meier1; Anja Bockmann2; Ronald Melki3; Luc Bousset3; 1ETH Zuerich, Zuerich, Switzerland; 2Institut de Biologie et Chimie des Proteines, Lyon, France; 3Laboratoire d’Enzymologie et

Biochimie Structurale, Gif-sur-Yvette, France Parkinson’s disease is amongst the most frequent and most devastating neurodegenerative diseases. It is tightly associated with the deposition of α-synuclein fibrils in the diseased brain. The field has been plagued by the difficulty to obtain samples of a single polymorph. We have obtained samples of two different pure forms. Here, we describe the spectra of the two polymorphs, both fibrillized at neutral pH, and compare their structural as well as their dynamical properties. One of those polymorphs has not been described so far. We will present the assignment of this new polymorph obtained under different assembly conditions.

Poster 317

Structural Studies of Aβ (1-42) in Fibrillar and Spherical Assemblies by SSNMR

Yiling Xiao1; Sudhakar Parthasarathy1; Masafumi Inoue2; Minako Hoshi2; Yoshitaka Ishii1; 1Univ. of Illinois at chicago,

Chicago, IL; 2Institute of biomedical research and innovation, Kobe, Japan

The 42-residue Alzheimer’s β (Aβ(1-42)) peptide misfolds into fibrils, and spherical non-fibrillar assemblies in diameters of 10-15 nm, called amylospheroid (ASPD). The strong aggregation propensity of Aβ(1-42) made it challenging to obtain fibrils with high homogeneity for structural analysis. It was even harder to isolate ASPDs for its meta-stable nature. We have made advance for SSNMR-based structural studies by preparing homogenous Aβ(1-42) fibrils via seeding method, and isolating ASPD-like assemblies in similar low salt condition. 13C SSNMR results indicate fundamental differences in the secondary structures for this fibril sample from those in the reported structures of Aβ(1-40) and Aβ(1-42) fibrils. Possible supramolecular assemblies of the Aβ(1-42) fibril and structural differences from the ASPD-like assembly will be discussed.

Poster 318

Pulse Sequences Optimized to Narrow 1H Resonances in Solid-state NMR Spectra of Membrane Proteins in

Phospholipid Bilayers George J. Lu; Stanley J. Opella; University of California,

San Diego, La Jolla, CA We demonstrate a magic sandwich based pulse sequence that narrows 1H amide resonance line widths to <300 Hz compared to the previously observed line widths of ~700Hz on the mercury transport membrane protein, MerF, which has two transmembrane helices. Interestingly, the line narrowing occurs only for membrane proteins in phospholipid bilayers where they undergo fast rotational diffusion, but not for immobile molecules such as peptide single crystals. The improvement in resolution in the 1H chemical shift dimension enables us to combine oriented sample (OS) solid-state NMR and magic angle spinning (MAS) solid-state NMR to determine the structure of membrane proteins in proteoliposomes.

Poster 319

Structural Topology of the Full-Length M2 Protein of the Influenza A Virus From Solid-State NMR



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Shu Yu Liao1; Yuan Zhang1; Antoine Loquet2; Sarah D. Cady1; Yongchao Su1; Mei Hong1; 1Department of Chemistry,

Iowa State University, Ames, IA; 2Max Planck Institute, Goettingen, Germany

The influenza M2 protein is important for the entry and budding of the virus. While the transmembrane domain of M2 has been extensively studied structurally, the structure of the full-length protein is still unknown. Using 2D 13C-13C and 3D NCACX and NCOCX experiments, we have sequentially assigned the 13C and 15N chemical shifts of 80 out of 97 residues of full-length M2. These chemical shifts indicate an a- helical conformation for the ectodomain but b-strand conformation for the cytoplasmic tail. Water-edited experiments indicate the position of the b-strand cytoplasmic tail relative to the membrane. This structure topology suggests possible modes of interactions between M2 and the matrix protein M1 and the structural basis for M2-mediated virus budding.

Poster 320

Solid-State NMR Studies of Protein-Induced Membrane Curvature and Application to the Influenza M2 Peptide

Tuo Wang; Sarah D. Cady; Mei Hong; Department of Chemistry, Iowa State Univeristy, Ames, IA

31P and 13C solid-state NMR is used to determine membrane protein partitioning into lipid domains with distinct curvatures. 1H T2 relaxation of lipids and water detected through lipid 31P and peptide 13C reveal the preferential binding of the peptide in different lipid domains, whereas 2D peptide 1H - lipid 31P correlation gives direct evidence of peptide-lipid interaction. Using these approaches, we studied the influenza M2 protein, which mediates virus budding by causing membrane curvature. The amphipathic-helix-containing M2(21-61) causes high-curvature membrane domains, whereas the TM peptide does not. 1H T2 relaxation and 1H-31P correlation data indicate that M2(21-61) preferentially binds to the high-curvature isotropic domain, which perturbs the transmembrane helix conformation, thus weakening drug binding to this domain.

Poster 321

Membrane Protein Structure and Topology in Supported Lipid Bilayers and Bicelles using Multidimensional Oriented and MAS Solid State NMR Spectroscopy

Kaustubh Mote; Gopinath Tata; Gianluigi Veglia; Univ of Minnesota, Minneapolis, MN

Determination of membrane protein structure in fully hydrated lipid bilayers by solid state NMR spectroscopy is a major challenge due to challenges in obtaining sufficient resolution and sensitivity. With the development of a new suite of sensitivity-enhanced oriented solid state NMR pulse sequences and the concurrent development of DUMAS (Dual Acquisition Magic Angle Spinning NMR) experiments allowed the determination restraints in order to determine the structure of membrane proteins de novo. In this study, we have used 15N CSA, 15N-1H dipolar couplings, 1H CSA from O-SSNMR and TALOS restraints from MAS-NMR to determine the complete structure and topology of sarcolipin in magnetically oriented bicelles as well as mechanically oriented lipid bilayers.

Poster 322 Structure and Interactions of 13C-Labeled Plant Cell

Walls by Multidimensional Magic-Angle-Spinning NMR Tuo Wang1; Marilu Dick-Perez1; Andrea Salazar2; Olga

Zabotina2; Mei Hong1; 1Department of Chemistry and Ames Laboratory, Ames, IA; 2Department of Biochemistry,

Biophysics & Molecular, Ames, IA Multidimensional 13C MAS NMR is used to study the structure and molecular interactions in 13C-labeled primary cell wall of Arabidopsis thaliana. Based on 13C resonance assignments, intermolecular cross peaks are identified in 2D and 3D 13C correlation spectra. Cellulose microfibrils, including the crystalline interior cellulose, exhibit numerous cross peaks with pectins, while hemicellulose has a small number of cellulose cross-peaks. Glycoprotein-pectin cross peaks are also observed. These results indicate a single network of all three polysaccharides, in which hemicellulose is entrapped in the cellulose microfibrils. The 2D spectra do not reach complete exchange even at 1.5 s, indicating that the polysaccharide network is inhomogeneous on the ~10 nm scale. Multidimensional SSNMR and isotopic labeling is thus applicable to complex bi omaterials.

Poster 323 Site-specific Conformation and Dynamics of Fibrillar

Polyglutamine Mutants by Magic-Angle Spinning NMR Cody L. Hoop; Karunakar Kar; Rakesh Mishra; Ravindra Kodali; Ronald Wetzel; Patrick C.A. van der Wel; Univ of

Pittsburgh, Pittsburgh, PA Expansion of CAG repeats coding for polyglutamine (polyQ) domains are found to play a role in at least nine human diseases, including Huntington’s Disease. These polyQ domains self-aggregate to form amyloid fibrils, the structure of which remains elusive. Extending our earlier investigations, we have employed multidimensional structural and dynamical measurements by magic-angle spinning NMR to probe conformational and motional changes that result from specific mutations in polyQ flanking domains as well as the amyloid core. The structural characteristics of these mutant fibrils are of interest for understanding not just the fibril structure, but also aspects of stability and dynamics as they correlate to analogous constructs examined in model animals.

Poster 324

NMR Relaxation Approach to Investigation of Plant Tissues

Nadezhda Sheveleva; Mari State Technical University, Yoshkar-Ola, Russian Federation

Nuclear Magnetic Resonance is a non-destructive rapid method that gives information about various morphological and physiological parameters of plants. Presented study was aimed to investigate the applicability of NMR relaxation for assessment of proliferative activity and also to determine optimal conditions of plant explants germination during cultivation at various stages of ontogeny. Such correct diagnostics shows up the possibility to significantly increase efficiency of culture media components selection and consequently to accelerate the breeding of plants.

Poster 325

Complete Atomic Resolution Structure of Amyloid Fibrils by DNP-Enhanced MAS NMR Spectroscopy:

Transthyrethin(105-115)



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Galia Debelouchina1; Marvin Bayro1; Anthony Fitzpatrick2; Vladimir Ladizhansky3; Marc Caporini1; Christopher Jaroniec4;

Vikram Bajaj1; Melanie M Rosay5; Cait MacPhee6; Werner Maas5; Chris Dobson2; Robert Griffin1; 1Massachusetts Institute of Technology, Cambridge, MA; 2University of

Cambridge, Cambridge, UK; 3University of Guelph, Guelph, ON; 4The Ohio State University, Columbus, OH; 5Bruker

BioSpin Corporation, Billerica, MA; 6University of Edinburgh, Edinburgh, UK

There are now examples of amyloid protofilament structural models in the literature but detailed information regarding the higher levels of structural organization within the fibrils is still lacking. Here, we report the first atomic resolution structure of a complete fibril, formed by an eleven-residue segment of the protein transthyretin (TTR). Our structure is based on 111 quantitative distance and torsion angle restraints, obtained with conventional and DNP-enhanced MAS NMR spectroscopy. These structural constraints allowed us to define not only the β-strand arrangement of the peptide into β-sheets and the β-sheet interface within each protofilament, but also to identify the nature of the protofilament-to-protofilament contacts that lead to the formation of the complete fibril.

Poster 326

Autocalibration Methods for Automated Biological Solid-state NMR Experiments

David M. Rice1; George Gray1; Krisztina Varga2; Andrew Nieuwkoop3; Ming Tang3; Chad Rienstra3; 1Agilent

Technologies, Santa Clara , CA; 2University of Wyoming, Laramie, WY; 3University of Illinois, Urbana-Champaign, IL

Solid-state methods for protein 1H, 13C and 15N assignments such as NCA, NCO, NCACX, etc require the calibration of multiple cross-polarization steps, as well a hard and soft shaped-pulse widths. Good-quality automatic calibrations should reveal probe and instrumental sensitivities that arise from RF heating or potential breakdown and they must deal with issues such as RF inhomogeneity. We have an ongoing project at Agilent, with our collaborators, to systemize the major solid-state biological experiments and to run them from the spectrometer queuing system. Autocalibration is part of this project. The poster will describe our practical approaches to automatic calibration for solid-state protein samples and show the results of experiments.

Poster 327

Hydrogen Bonding Network in Bone by Solid State NMR Spectroscopy

Neeraj Sinha; Ratan K Rai; Chandan Singh; Centre of Biomedical Magnetic Resonance, Lucknow, India

Water is one of the important components of bone. It acts as pore-filling fluid in bone between organic and inorganic part. The possible role of water in bone structure has not been fully explored. We will be presenting the possible ultra-structural changes in bone by solid state NMR (SSNMR). 1H high-resolution high-speed magic-angle spinning solid-state NMR provides information on the effect exerted by various water level contents present in bone. Four samples of various degrees of dehydration and H/D exchanged bone samples are compared and the possible change in 1H chemical shift at higher spinning speed will be presented. These study shows effect of hydration on the molecular mobility of collagen in cortical bone samples.

Poster 328 Paramagnetic Relaxation Enhancement Magic-Angle Spinning SSNMR Studies of Alpha-Synuclein Fibrils

Marcus Tuttle; Andrew Nieuwkoop; Joseph Courtney; Gemma Comellas; Luisel Lemkau; Deborah Berthold; Shin Lee; Jae

Kim; Julia George; Chad Rienstra; University of Illinois at Urbana-Champaign, Urbana, IL

Fibrils of the 140 amino acid protein α-Synuclein (AS) are the primary constituent of Lewy Bodies, the pathological hallmark of Parkinson’s disease. While current SSNMR methodologies have provided many structural insights into AS, lack of unambiguous long-range structural restraints have proved to be an impediment to differentiating models of the tertiary and quaternary structure. Here we present results providing long-range structural insights from nitroxide spin-labeled cysteine mutants of AS using paramagnetic relaxation enhancement (PRE) magic-angle spinning (MAS) SSNMR. Additionally, we show that judicious choice of cysteine mutagenesis within the structured region of AS is crucial to preserve the overall fold observed in wild-type.

Poster 329

Identifying Inter-Residual Resonances in Crowded 2D 13C-13C Correlation Spectra of Membrane Proteins by Solid-

State MAS NMR Difference Spectroscopy Yimin Miao1, 2; Timothy A. Cross1, 2; Riqiang Fu1; 1National

High Magnetic Field Laboratory, Tallahassee, FL; 2Department of Chemistry and Biochemistry, FSU,

Tallahassee, FL A "difference spectroscopy" has been introduced for identifying inter-residual resonances in crowded 2D 13C-13C correlation solid-state MAS NMR spectra of membrane proteins. 13C-13C DARR spectrums of 13C, 15N uniformly labeled full length M2 protein in DOPC/DOPE lipids at pH6.6 with a series of mixing time had been recorded. Compared to the hardness of identifying residual correlations in the long mixing time spectra with poor resolution, more inter-residual resonances were identified after making "difference spectroscopy" between short and long mixing time spectra, with negative and positive peaks representing the relatively short and long distance correlations, respectively. This method is very useful to establishing inter-residual connectivity in spin diffusion experiments where stronger intra-residual resonances and weaker inter-residual resonances coexist in the same spectrum.

Poster 330

Elucidating the Structure and Functional Dynamics of Membrane-Bound Tissue Factor by Solid-State NMR Kristin Nuzzio; John Boettcher; Rebecca Davis-Harrison; James Morrissey; Chad Rienstra; University of Illinois at

Urbana-Champaign, Urbana, IL Proteins involved in the blood coagulation cascade are of vital biomedical importance, and most essential blood-clotting reactions occur preferentially on phospholipid membranes. The blood coagulation cascade is initiated when Factor VIIa (FVIIa) binds to the integral membrane protein, tissue factor (TF). Here, the nanocrystalline and membrane-bound forms of TF are investigated using solid-state NMR. The solid-state chemical shifts of nanocrystalline TF agree well with the previously published solution NMR chemical shifts as well as with X-ray crystal data. Our preliminary results indicate that upon membrane binding, TF retains its primarily beta-sheet



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secondary structure; however, perturbations are observed in several regions that are thought to be involved in the TF/FVIIa putative exosite near the membrane surface.

Poster 331

Solid-state NMR Structural Analysis of Symfoil-1: A Controllable Amyloid-forming Protein

Liam Longo; Florida State University, Tallahassee, FL Symfoil-1 is a unique model system in which the conformational state of the protein can be controllably shifted from a stable globular protein to a self-assembled amyloid state. We probed the molecular structure of self-assembled Symfoil-1 using 2D fpRFDR, 2D RAD and 3D NCACx/NCOCx experiments. The 2D fpRFDR ssNMR spectra exhibit linewidths (~2 ppm, full width at half maximum) that are indicative of a well-defined structure and local structural order. The 2D RAD spectra contain information about the molecular fold within the amyloid state, through crosspeaks between non-adjacent residues in the sequence. These data, in conjunction with mutagenesis studies, will allow for a precise identification of the amyloidogenic region within Symfoil-1, as well as the energetic contribution of individual residues.

Poster 332

Hydrogen-Deuterium Exchange Experiments in Proteorhodopsin

Emily Ritz1; Lichi Shi2; Leonid Brown1; Vladimir Ladizhansky1; 1University of Guelph, Guelph, Canada; 2University of

Toronto, Toronto, Canada Proteorhodopsin (PR) is a transmembrane heptahelical proton pump. Although many steps of its proton transport are similar to those in its homolog bacteriorhodopsin, there are differences related to the proton release step, along with the proposed existence of a hydrophilic cavity. In order to map PR's solvent-accessible surface, we performed hydrogen-deuterium (H/D) exchange experiments using two samples of PR grown using 1,3-13C and 2-13C labeled glycerol. The amide protons at exposed sites on the protein undergo exchange with deuterium in the solvent, leading to signal attenuation or disappearance in multidimensional chemical shift correlation experiments (NCA and NCO). We use these experiments to detect the water accessible surface site-specifically, and gain insight into the proton transport mechanism of PR.

Poster 333

Kinects of the Calcium Phosphate Formation on Bioglass Surface: 31P MAS NMR Study

João H. Lopes; Celso A. Bertran; Italo O. Mazali; Alviclér Magalhães; IQ UNICAMP, Campinas, Brazil

In the last decades a revolution in public health has resulted in a new challenge for society, in order to maintenance the quality of life in an aging population. Research in the field of biomaterials has developed a wide range of materials for hard and soft tissue regeneration. 45S5 bioglass shows the capability to bond direct to bone through a layer of hydroxycarbonate apatite (HCA). Some issues involving the kinetics of formation of amorphous calcium phosphate and its structural evolution to HCA. In this work HCA layer formation was studied on the surface of bioglass 45S5 and in a sample 45S5 enriched with Calcium in the presence of SBF using 31P as a probe to the kinetic studies.

Poster 334 High-resolution Structure of a Seven-helical Membrane

Protein Determined by Solid State NMR Shenlin Wang1; Lichi Shi2; Izuru Kawamura4; Kwang-Hwang Jung3; Leonid Brown1; Vladimir Ladizhansky1; 1University of Guelph, Guelph, Canada; 2University of Toronto, Toronto, Canada; 3Sogang University, Seoul, Korea; 4Yokohama

National University, Yokohama, Japan Anabaena sensory rhodopsin (ASR) is a 7TM photosensor involved in the regulation of expression of several genes related to the utilization of light. In this abstract we present high-resolution structure of ASR determined by SSNMR. 3D spectroscopy on ASR grown on 2-13C and 1,3-13C labeled glycerol allowed obtaining a large number of structural restraints. SSNMR structure agrees with the X-ray structure on the extracellular side, but differs widely on the cytoplasmic side, where helices A, B, E, F are tilted away from the bundle. H/D exchange indicates that these helices are more water exposed, indicating increased dynamics of the cytoplasmic half. To better constrain the cytoplasmic side we are conducting additional PRE measurements, which will be presented in this abstract.

Poster 335

Implementing Fibril Symmetry Restraints in CYANA for Structure Calculation of Amyloid beta Fibrils from Solid-

State NMR Data Matthias Huber1; Anne Schuetz1; Oxana Ovchinnikova1; Anja Bockmann2; Rudi Glockshuber1; Peter Guentert3; Beat Meier1; 1ETH Zurich, Zurich, Switzerland; 2IBCP-CNRS, Lyon, France;

3J.W. Goethe University, Frankfurt, Germany We present solid-state NMR data from fibrils of Amyloid β 1-40 E22δ (the Osaka mutant leading to familial Alzheimer’s disease) which are highly ordered and yield line widths in the order of 0.5 ppm. We compare the spectra of Aβ fibrils with those from fibrillar HETs and microcrystalline Ubiquitin and discuss the relative importance of different restraint classes (torsional angle, h-bond as well as intra- and intermolecular distance restraints) for structure calculation of the different proteins. We show how fibril symmetry can be enforced with CYANA during the calculation fibril segments by adding pseudo energy terms that ensure symmetric packing of monomers along the fibril axis and in the transverse cross-section.

Poster 336

Solid-state NMR Characterization of Cholesterol-binding Caveolin Fragments in Mixed Lipid Membranes

Cody Hoop; V N Sivanandam; Ravi Kodali; Matthew Srnec; Patrick C.A. Van Der Wel; Univ of Pttsburgh, Pittsburgh, PA

Magic angle spinning and static solid-state NMR methods were used to characterize the conformation and membrane interaction of membrane-bound fragments of the protein caveolin-1. This protein is implicated in a number of human diseases and plays a critical role in cholesterol trafficking and the formation of cholesterol-rich plasma membrane domains known as caveolae. Its scaffolding domain carries a multiplicity of functionalities, notably including conserved residues involved in the cholesterol binding. Our solid-state NMR experiments permitted the direct conformational characterization of this domain in presence of high (50%) cholesterol concentrations and provided insights into the polypeptide structure and its effects on the membrane.



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Poster 337 Membrane Protein Immersion Depth Estimation: 31P MAS

SSNMR PRE Approach and MD Verification Sergey Maltsev; Miami University, Oxford, OH

Site directed spin labeling (SDSL) with a paramagnetic molecule attached to a lipid proved to be effective to provide quantitative information on spin-label depth inside a multilamellar vesicle(MLV) membrane. Here we present the next step of the technique – spin labeling a protein inside MLV membrane. Experimental results show a linear behavior of 31P paramagnetic relaxation enhancement (PRE) rates of the phospholipid headgroup as spin label moves towards the center of the membrane, making it easy to interpret the results and thus get protein depth and conformation information. Molecular dynamics simulations were performed in order to verify the experimental results and to get PRE correlation times for different positions of spin label along the protein.

SOLIDS: INORGANICS & MATERIALS, 338 - 357

Poster 338

Application of 209Bi and 7Li Solid-State NMR to the Characterization of Tetrametallic Coordination

Complexes Marcus Drover; Celine Schneider; Louise Dawe; Nduka Ikpo;

Francesca Kerton; Memorial University of Newfoundland, St John's, Canada

A series of dimeric, tetranuclear lithium amine-bis(phenolate) complexes were examined using solution and solid-state 7Li NMR spectroscopy. Variable temperature 7Li solution NMR revealed that these compounds are labile, readily collapsing to afford two dimeric entities at high temperature. Additionally, 7Li MAS NMR provided pivotal information regarding the lithium coordination environment, such as quadrupolar couplings and chemical shift tensors. Reaction of BiCl3 with these lithium complexes provided monometallic and tetrametallic bismuth compounds which were probed using 209Bi solid-state NMR. To this end, ultra wide-line measurements such as frequency-stepped Hahn-echo and QCPMG techniques were applied. 209Bi SSNMR was also used to characterize some simple Bi-containing salts. Relaxation times, quadrupolar couplings and chemical shift anisotropy tensors were also extracted from 209Bi data.

Poster 339

MAS Effect on Molecular Motion of SBR in SBR/Si Composites

Atsushi Asano; Shunsuke Hori; Masashi Kitamura; Chikako T. Nakazawa; Takuzo Kurotsu; National Defense Academy,

Yokosuka, Japan We investigated the MAS effect on the molecular motion of styrene-butadiene rubbers (SBR) filled with SiO2 (SBR/Si composite) though solid-state 1H MAS NMR measurements.The temperature dependence of the 1H spin-lattice relaxation time (T1

H) revealed that the T1H minimum

increases with the MAS rate. The empirical fitting to the temperature dependence of T1

H revealed that the molecular motion does not change significantly until a MAS rate of 20 kHz. At a MAS rate of 25 kHz, the motional mode changed considerably.The plot of the estimated centrifugal pressure vs. the T1

H minimum resembled the stress-strain curve. This result enables the detection of macroscopic physical deformation via the microscopic parameter T1

H.

Poster 340 in situ High Pressure and Temperature NMR of CO2 in

Geosequestration and Materials Science Studies J. Andrew Surface; Jeremy Moore; Philip Skemer; Mark

Conradi; Sophia E. Hayes; Washington Univ, St. Louis, MO Materials for carbon capture and sequestration are under investigation to selectively collect, use, and/or store carbon dioxide. We are developing in situ (static) 13C NMR equipment, which can measure reaction kinetics, diffusion, chemical exchange, and quantify reactant/product. We can provide a special "window" to analyze these systems as they react at moderate pressures (0-250 atm) and temperatures (-70C-250C). To date, we have performed preliminary proof-of-concept work on materials that selectively adsorb CO2 and have analyzed the dissolution and resultant chemical reactions of supercritical CO2 in water and brine-containing powdered rock. Herein we describe our newly developed NMR instrumentation and techniques as well as recently obtained results.

Poster 341

Solid-state NMR Characterization of Polymeric Membrane Materials

Sungsool Wi1, 2; Ying Chen1, 2; 1Virginia Tech, Blacksburg, VA; 2Virginia Tech, Blacksburg, VA

We have utilized solid-state NMR (SSNMR) spectroscopy to investigate the dynamic and morphological properties of polymeric membrane materials fabricated for fuel cell and reverse osmosis (RO) applications to understand the fundamental correlations to the various types of conventional macroscopic properties. Our particular emphasis was given on the study of polymeric chain motions and their correlations to the molecular transport properties in the polymer matrix that would play a central role in the fuel cell and RO membrane sciences. By carrying out collaborations with synthesis and processing experts we optimize the structure and morphology of the polymeric membrane material to regulate the dynamic characteristics of polymer chains, which would control the rate of molecular diffusion in the polymer matrix.

Poster 342

MAS NMR Study of VX, GD, and HD Reactions with Zr(OH)4

Gregory Peterson1; Teresa Bandosz2; Camille Petit2; Joseph Rossin3; George W. Wagner1; 1U.S. Army ECBC, Apg, MD;

2City College of New York, New York, NY; 3Guild Associates, Inc., Dublin, OH

MAS NMR studies examining the reactions of VX, GD, and HD with Zr(OH) 4 in situ reveal that all three agents undergo hydrolysis reactions with the material - the reaction of VX being particularly fast, exhibiting a half-life of a minute or less. The rapidity of the VX reaction is attributed to both the abundance and nature of the hydroxyl groups of Zr(OH) 4, which exhibit both acidic and basic character. Evidence for the latter is provided by the observation of minor elimination products for HD. For the observed facile reaction of VX, it is proposed that protonation by acidic hydroxyl groups of Zr(OH)

4 leads to catalytic hydrolysis - a reaction analogous to the ethyl methylphosphonate (EMPA)-autocatalyzed water-reaction.



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Poster 343 Q (3) Site Variations in a Mixed Potassium/Magnesium

Glass using Magic-Angle Flipping (MAF) NMR Eric G. Keeler1; Kevin J. Sanders1; Derrick C. Kaseman1;

Philip J. Grandinetti1; Jay H Baltisberger2; 1The Ohio State University, Columbus, OH; 2Berea College, Berea, KY

In this poster we present new data on cation clustering in mixed potassium and magnesium tetra-silicate glasses. We examined the degree of modifier cation clustering in a range of glass compositions with 29Si magic-angle flipping (MAF) NMR at natural abundance. We used CPMG echo train acquisition to enhance sensitivity due to the low isotopic abundance and NMR frequency. We found that doping the samples with Cu(II) reduced the relaxation delay enough to allow a full MAF spectrum to be acquired in 4 to 6 days. In agreement with the previous 17O study of this glass by Farnan and coworkers in 1992, these glasses appear to have significant ordering where the cations cluster as either pure potassium regions or mixed regions.

Poster 344

ex situ 13C MAS NMR Studies of Water Saturated Supercitical CO2 Reacted with Natural Forsterite

Mary Hu; Odeta Qafoku; Ju Feng; Bruce W. Arey; Andrew R. Felmy; Jian Zhi Hu; Pacific Northwest National Laboratory,

Richland, WA We report first solid state 13C MAS NMR analysis of reaction products obtained on water saturated supercritical CO2 reacted with natural forsterites under the conditions that are relevant to geological carbon sequestration, i.e., at 35 °C and 50 °C. We found that at 35 °C, the primary metal carbonation products were nesquehonite (MgCO3.3H2O). In contrast, at 50 °C and after 14 days of reaction, the major reaction products were magnesite (MgCO3). The observation that magnesite can form at 50 °C implies that water recycling may be important in determining the rate and extent of mineral carbonation in a wide range of potential CO2 storage reservoirs. 13C and 29Si results from synthetic forsterite under similar experimental conditions will also be reported.

Poster 345

Water Behavior in Hydrophilic Channels of Hot-Pressed Polymer Electrolyte Membranes Investigated by 2H NMR

Spectroscopy Oc Hee Han1, 2; Sang Man Lee1; Ryeo Yun Hwang2; 1Daegu Center, Korea Basic Science Institute, Daegu, Republic of Korea; 2GRAST, Chungnam National University, Daejeon,

Republic of Korea 2H NMR spectroscopy has been extensively employed for the study of ordering of molecules such as liquid crystal molecules by observing the molecules themselves or using probing molecules. Hydrophilic channel structures of PEMs were also investigated by determining residual quadrupole coupling values of 2H2O in PEMs. However, mainly stretched polymers and PEMs have been studied. In this work, 2H2O in hot-pressed Nafion 117 samples was investigated with 2H NMR spectroscopy and compared with the 2H NMR data of Nafion 117 without any stress applied and stretched Nafion 117 to investigate how hot-pressing affects the hydrophilic channels in Nafion 117.

Poster 346 Solid-State NMR Nuclear Magnetic Resonance

Investigation of Poly(Ethylene Oxide) Based Polyether-ester-sulfonate Ionomers

David Roach1; Karl Mueller1, 2; 1Penn State University, University Park, PA; 2Pacific Northwest National Laboratory,

Richland, WA Nuclear magnetic resonance spectroscopy has been utilized to investigate the structure and dynamics of poly(ethylene oxide)-based sulfonate ionomer samples that have low glass transition temperatures. These ionomers are made from polyethylene glycol with Mn = 600 and a varying ratio of dimethyl 5-sulfo-isophthalate lithium or sodium salt to neutral dimethyl isophthalate producing a range (6%, 11%, 17%, 100%) of ion contents. They are of interest because PEO solvates the cations and allows ion conduction to be studied. Additionally, these materials are viscous, amorphous liquids with Tg far below room temperature, which facilitates thermal equilibration of the system. NMR relaxation time measurements, cross-polarization dynamics, 13C linewidths, and Li self-diffusion constants are discussed in the context of polymer structure and dynamics.

Poster 347

Selenide Glasses Studied by 77Se Solid-state 1D and 2D NMR

Michael Deschamps1; Bruno Bureau2; Guang Yang2; Claire Roiland2; Eric Furet2; Laurent Le Pollès2; Philippe Corcos3;

Dominique Massiot4; 1Université d'Orléans, Orleans, France; 2Université de Rennes, Rennes, France; 3CortecNet, Voisins-

Le-Bretonneux, France; 4CNRS-CEMHTI, Orléans, France 77Se MAS-NMR is used to study selenide glasses, allowing the characterization of X-Se-Y motives. However, 77Se NMR suffers from low 77Se natural abundance (7.6%) and long T1's (>30s). Two strategies can be used : first, the use of CPMG acquisition with trains of rotor-synchronized 180° pulses during the magnetization detection has been tested on AsxSe1-x glasses; second, 77Se isotopic enrichment, which was realized for GexSe1-x, considerably increases the sensitivity of the NMR experiment, especially as these glasses suffer from extremely long longitudinal relaxation times. Moreover, it also allows recording 2D 77Se INADEQUATE spectra, which can be used for the identification of the strongly overlapping 77Se lines and the characterization of the spatial distribution of Ge/Se-Se-Ge/Se molecular motives.

Poster 348

Comparison of 19F qNMR, Absolute Fluorescence, and Absorption Measurements of Dye Concentrations in

Fluorescent PS Particles Christian Jaeger; Alexandra Huber; Ute Resch-Genger;

Christian Wuerth; Thomas Behnke; BAM Federal Institute of Materials Research, Berlin, Germany

Fluorescent nanometer-sized particles are important for an increasing number of applications of optical techniques in life sciences like large-scale analysis of biological systems such as DNA, multiplexed fluorescence assays, and cancer-related biomarker analysis in vivo. This background triggered the idea to develop a versatile procedure for correlating optical properties to the number of dye concentration using quantitative NMR. 1 µm-sized polystyrene particles encapsulating the dye coumarin 153 was investigated by 19F NMR to quantify the dye concentration



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(mol dye/ mol PS, mol dye/gram sample). Results are compared with those of colorimetric dissolution. Sample preparation (elimination of sample inhomogeneity), and quantification strategy including uncertainty estimation using PTFE (reference standard) are described. Dye concentrations down to 10-50 µmol/mol can be measured.

Poster 349

Recent Advances in 195Pt Solid-State NMR Bryan E. G. Lucier1; Alex R. Reidel1; Kristopher J. Harris1; Jochen Autschbach2; Robert W. Schurko1; 1University of

Windsor, Windsor, Canada; 2State University of New York at Buffalo, Buffalo, NY

Solid-state NMR (SSNMR) experiments on NMR-active transition metal centers are powerful structural probes for a wide array of materials. In particular, 195Pt SSNMR has been widely used in the characterization of Pt-containing systems. SSNMR 195Pt powder patterns of square-planar platinum(II) compounds give valuable information on the anisotropic chemical shielding and local electronic structure; however, they are normally very broad and require time-consuming experiments. Recently, we introduced the WURST-CPMG pulse sequence to drastically decrease experimental times for the acquisition of broad powder patterns. We have used 195Pt SSNMR, in concert with first principles calculations, to gain insight into the nature and strength of Pt-Pt metallophilic interactions in model compounds, and also to explore local structural environments of cisplatin and related species.

Poster 350

A Study of Transition-Metal Organometallic Complexes using 35Cl Solid-State NMR, 35Cl NQR and First-Principles

DFT Calculations Karen Johnston; Christopher O'Keefe; Robert Schurko;

University of Windsor, Windsor, Canada Our research aims to provide a multidisciplinary approach to the characterization of common transition-metal organometallic complexes; more specifically, those routinely used as homogeneous and heterogeneous catalysts. Such complexes are normally investigated via 1H and 13C solid-state NMR (SSNMR) and X-ray diffraction (XRD) techniques. We are exploring the use of 35Cl (spin-3/2) SSNMR and 35Cl NQR with density functional theory (DFT) calculations for the identification and differentiation of these systems. Using these techniques, it is possible to gain structural insight into systems with common metal-chlorine bonding motifs that may not be amenable to standard characterization using routine SSNMR or XRD methods. For example, recent work has demonstrated it is possible to distinguish between bridging and terminal Cl positions using 35Cl SSNMR.

Poster 351

Distribution of Aluminium in Zeolites: T-sites Resolved by 27Al Single Crystal Solid State MAS NMR

Ernst Van Eck; Radboud University Nijmegen, Nijmegen, Netherlands

The distribution of aluminium atoms within the zeolite silicate lattice is important as it determines the performance of the zeolites as a catalyst. For a microcrystalline powder it can be possible to resolve the various T-sites present in a zeolite with 29Si NMR. For aluminium however, this has remained a challenge as the resonances are intrinsically broadened by the quadrupolar interaction and often overlap strongly. Here

we represent experiments on zeolite single crystals would greatly enhance resolution. 2D MQMAS experiments at multiple fields in combination with DFT calculations of the chemical shift and the quadrupole tensors allows assignment of the T-sites of ferrierite and hence the distribution of aluminium over the lattice to be determined directly for the first time.

Poster 352

Molecular Structural Study of Thin-film Boron Carbide Wenjing Li; Michelle Paquette; Bradley Nordell; Anthony

Caruso; Nathan Oyler; UMKC, Kansas City, MO Boron-rich carbides have very unique characters that can be applied in developing thermal, electrical, and mechanical materials. To date, no clear understanding about the molecular structure and the formation mechanism of thin-film boron carbides has been established. Here, we demonstrate our progress in the molecular structural study of amorphous hydrogenated boron carbide thin-film made by applying the plasma-enhanced chemical vapor deposition (PECVD) method to a single-source precursor orthocarborane (C2B10H12). To investigate physical structure of a-BxC:Hy thin-films we applied solid-state magic angle spinning nuclear magnetic resonance (MAS-NMR) methods along with elemental analysis and Fourier transform infrared (FTIR) spectroscopy. Ab initio calculations were also performed to compare with the experimental results in order to propose a structural model.

Poster 353

Enhancing Resolution in 13C CP-MAS NMR using Single Crystals: Application to Model Octaethyl Porphyrin

Systems Sneha Dugar1, 2; Riqiang Fu1; Naresh Dalal1, 2; 1National High

Magnetic Field Laboratory, Tallahassee, FL; 2Florida State University, Tallahassee, FL

We observed that the use of a single crystal instead of powder samples lead to two fold enhancement in resolution. 13C CP-MAS measurements were done on octaethyl porphyrin (OEP) and its analogs, ZnOEP and NiOEP (300MHz, 1H). The spectrum of powder NiOEP showed a single peak for CH2/CH3 and Cα/Cβ carbons. On using a single crystal, the peaks from the CH2 carbons and the Cα/Cβ were split into a doublet. These multiple peaks could be assigned and were attributed to crystal packing and intermolecular π electron cloud effect: in agreement with X-ray structure. Similar studies were done on ZnOEP and OEP. Thus, the use of single crystals could prove to have a wider impact than expected.

Poster 354

A Solid-state NMR and Theoretical Study of Li-assisted Dehydrogenation Mechanism of Ammonia Borane

Takeshi Kobayashi1; Ihor Z. Hlova1, 2; Niraj K. Singh1; Vitalij K. Pecharsky1, 2; Marek Pruski1, 2; 1Ames Laboratory, Ames, IA;

2Iowa State University, Ames, IA The reaction mechanism of thermal dehydrogenation of the mixture of lithium aluminum hydride and ammonia borane (Li3AlH6-3NH3BH3) has been studied in detail by solid-state NMR measurements, including 1D 27Al and 11B DPMAS, as well as 2D 11B MQMAS, and theoretical DFT calculations. The NMR spectra showed that the dehydrogenation of ammonia borane (AB) in the presence of Li3AlH6 takes a different path than the thermolysis of pristine AB, which involves ammonia



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diborane. Instead, part of AB in the mixture dehydrogenates by forming an intermediate compound (LiAB) x (AB) 1-x, which accelerates the subsequent formation of branched polyaminoborane species and further release of hydrogen. The experimental results were confirmed by DFT calculations of the chemical shifts and quadrupolar parameters.

Poster 355

Acid-exchanged Layered Niobates: Local Structural Investigation via Dipolar Recoupling

Ting Liu; Clark University, Worcester, MA Local structures in five different acid-exchanged layered niobates, HNb3O8, HLaNb2O7, H4Nb6O17, HLa2NbTi2O10, and HCaLaNb2TiO10 were investigated by means of a variety of solid-state NMR techniques. 93Nb Multiple-quantum MAS (MQMAS) and static multi-field VOCS methods were utilized to examine Nb environments in NbO6 octahedra. Local distortions were found in all compounds. Static cross polarization (CP) and transfer of population in double-resonance (TRAPDOR) experiments were used to study H-Nb proximity through space. Symmetry-based rotational-echo saturation-pulse double-resonance (S-RESPDOR) and quadrupolar heteronuclear dipolar recoupling experiments were used to extract H-Nb dipolar coupling constants by analytical analysis of the dipolar dephasing curves. Structural re-arrangements, especially on the surface (interlayer space) will be proposed. Differences in proton locations and correlation with properties will be discussed.

Poster 356

Water-polyethylene Glycol Interaction in Nafion Studied with Solid State NMR Spectroscopy, NMR Micro-imaging

and Molecular Dynamics Simulation Rui-Yi Huang; Zhen Wu; Ren-Hao Cheng; Shangwu Ding;

National Sun Yat-sen University, Kaohsiung, Taiwan The 1H chemical shift, relaxation rate and diffusion coefficient of water and PEG in Nafion reveal extraordinary structural and dynamic properties of water and PEG in a confined, acidic space. Water molecules are found to be attracted to PEG from sulfonate sites and have longer rotational correlation time as the concentration of PEG increases. Variable temperature relaxation data show significant deviation from Arrhenius behavior. Addition of PEG improves mechanical stability and reduces swelling caused by methanol, but the AC impedance of Nafion increases with the concentration of PEG. Based on these experimental data and molecular dynamics simulation, a model is proposed for describing water and PEG in Nafion, which facilitates a better understanding of proton transport in this important membrane.

Poster 357

7Li NMR with 0.1MHz MAS Ago Samoson1, 2; Radostina Stoyanova3; Tiit Tuherm1; 1TUT,

Tallinn, Estonia; 2University of Warwick, Coventry, UK; 3Institute of General and Inorganic Chemistry, Sofia, BG

Li-ionic conductors and energy storage by definition introduce in the composition nemesis of NMR- paramagnetic atoms. We have performed a series of measurements at different fields and spinning speeds on transition metal oxides with compositions LiCo1-2xNixMnxO2 offering a representative variety of Li environments since the nickel ions are in the oxidation state 2+, while the cobalt and manganese ions

adopt oxidation states: 3+ and 4+. Reliable spectra at common 4.7T can be achieved when the spinning rate approaches 100 kHz. At lower, 2.35T field, already 60 kHz of spinning give similar results.

SOLIDS: METHODS, 358 - 381

Poster 358

Sensitivity and Resolution Enhancement with Spinning Micro-Coil in NMR Spectroscopy

Wealen Ke; Zhen Wu; Ren-Hao Cheng; Shangwu Ding; National Sun Yat-sen University, Kaohsiung, Taiwan

This work shows the new opportunities offered by combining magic angle coil spinning (MACS) and surface coil detection in NMR spectroscopy (of both solids and liquids) and NMR micro-imaging. The design specifications of the micro NMR probes for common nuclei 1H, 23Na, 31P and 79Br have been identified. High RF field up to 700 kHz has been achieved so that both spin-1/2 and quadrupolar nuclear systems can be detected with high resolution. We have tested different methods for mounting the samples and compared their performance. Surface coil detection method is found to offer best sensitivity with good resolution. We have also demonstrated the practical applications in detecting microscopic quantity of compositions in materials and biological systems.

Poster 359

Sideband Selective Double Frequency Sweeps for Sensitivity Enhancement of MAS NMR of Half Integer

Quadrupolar Nuclei Mithun Goswami; Jan van Bentum; Arno Kentgens; IMM,

Radboud University, Nijmegen, Netherlands Sensitivity enhancement based on adiabatic inversion of a single set of satellite transition sidebands under magic angle spinning will be described and applied in 27Al MAS NMR of minerals with various 27Al sites. Overall enhancements of ~3 are achieved by applying this sideband selective Double Frequency Sweep (ssDFS) prior to a selective excitation of the central transition. Repetitive application of the ssDFS and signal readout without allowing for spin-lattice relaxation leads to sensitivity enhancements of up to 5 even for the most distorted site (CQ~18MHz) in zoisite. Based on the spread of satellite spinning sidebands the position of the sweep can be exploited for spectral editing by selective enhancement of based on the different size of the quadrupolar interaction.

Poster 360

Exploiting 13C NMR Magnetization by Uniting Cross- and Direct-Polarization: An Efficient Scheme for Soil Organic

Matter Studies in the Solid-State Denis Courtier-Murias; Ronald Soong; James G. Longstaffe;

Myrna J. Simpson; Andre J Simpson; Department of Chemistry, University of Toronto, Toronto, Canada

Soils are the most important carbon reservoir in the terrestrial carbon cycle and arguably essential to all life on earth. Despite their importance, soil structure and formation processes are not fully understood molecularly. One reason for the lack of understanding is the complexity of soils and lack of analytical approaches that provide a comprehensive molecular overview. NMR spectroscopy is ideal for study of such complex systems. In particular, 13C cross-polarization magic-angle-spinning (CP/MAS) has proven highly sensitive



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and suitable for the inter-comparison of soil samples. Here an NMR scheme that combines CP and single pulse (SP) experiments is applied to various soils. This experiment, termed “CPSP”, is more sensitive and leads to better representation of non-protonated carbon than CP/MAS alone.

Poster 361

Time-domain NMR Method of Water Content Determination of Wood and Peat Based Fuels for On-line

Process Control Ekaterina Nikolskaya1, 2; Yrjo Hiltunen2; Leonid Grunin1; 1Mari State Technical University, Yoshkar-Ola, Russian Federation;

2University of Eastern Finland, Kuopio, Finland The water content is an important parameter for biofuel quality evaluation. The standard method based on drying and weighting requires a long time for water content determination. The best decision of the problem is to implement on-line system for rapid and precise definition of biofuels water content. Time-domain NMR (TD-NMR) as a modern promising tool of physical and chemical analysis of substances with wide area of possible industrial applications has been used. The results of our study demonstrate sufficient accuracy for TD-NMR method to be applied both in laboratories and in industry for express water content determination of wood and peat based fuels without additional calibration.

Poster 362

Refocused-CW Decoupling for Solid-State NMR Joachim M. Vinther1; Anders B. Nielsen1; Navin Khaneja2; Niels Chr. Nielsen1; 1Interdisciplinary Nanoscience Center, Aarhus University, Aarhus, Denmark; 2Harvard University,

Cambridge, MA Spectral resonances in solid-state magic-angle spinning (MAS) NMR spectra are broadened due to heteronuclear and homonuclear dipolar couplings to and among the protons. This results in poor resolution, overlapping peaks and ambiguous resonance assignments. Average Hamiltonian Theory (AHT) has been used to third order to determine the interactions remaining during CW-decoupling. For the 2-spin system of 1H-13C the analysis points on one second order term and two third order terms. The new type of sequences presented refocuses the development due to these terms by rotor-synchronized insertion of differently phased π-refocusing pulses during the CW irradiation. Larger spin systems, where refocusing of all terms is not possible, will as well be addressed.

Poster 363

Enhanced Sensitivity by Nonuniform Sampling Enables Multidimensional MAS NMR Spectroscopy of Protein

Assemblies Christopher Suiter1, 2; Sivakumar Paramasivam1; Guangjin

Hou1, 2; Shangjin Sun1, 3; Melissa Palmer4; Jeffrey C. Hoch5; David Rovnyak4; Tatyana Polenova1, 2; 1University of

Delaware, Newark , DE; 2Pittsburgh Center for HIV Protein Interactions, Pittsburgh, PA; 3Center for Cancer Research, NCI, Frederick, MD; 4Bucknell University, Lewisburg , PA;

5Univ of Connecticut Health Ctr, Farmington, CT We investigate sensitivity and resolution in multidimensional MAS NMR obtained by NUS and introduce Maximum Entropy Interpolation (MINT) processing. We demonstrate on the tripeptide MLF and thioredoxin

reassembly that with NUS at least one-and-a-half to two-fold sensitivity enhancement can be attained without compromising resolution. The extent of sensitivity enhancement is dependent upon the choice of the NUS sampling schedule. In thioredoxin reassembly, NUS permits acquisition of a high-quality 3D-NCACX spectra, which are inaccessible with conventional sampling due to long experiment times. Of critical importance, issues hindering NUS-based sensitivity enhancement in 3D-NMR of liquids are mitigated in solids where theoretical enhancements of 3-4 fold are accessible. NUS/MINT is anticipated to be applicable and advantageous for multidimensional MAS NMR spectroscopy of biomolecules.

Poster 364

3D Correlation of Quadrupolar Anisotropy, Shielding Anisotropy, and Isotropic Shielding

Brennan Walder1; Michael Davis1; Krishna Dey1; Jay H Baltisberger2; Philip J. Grandinetti1; 1The Ohio State

University, Columbus, OH; 2Berea College, Berea, KY Using the formalism of symmetry pathways and the PASS equations, we have designed a technique that achieves a complete separation and three dimensional correlation of the quadrupolar anisotropy, shielding anisotropy, and isotropic shielding frequencies. With conventional PASS processing, the shielding anisotropy dimension can be separated from the other two, and through the use of TOP processing on the remaining mixed isotropic shielding/quadrupolar dimension, a complete decomposition of the spectrum into three orthogonal interaction dimensions is achieved.

Poster 365

Multiple-Acquisition in Biological Solid-State NMR: Exploitation of Polarization from Different Spin Species Berit Paaske1; Morten Bjerring1; Hartmut Oschkinat2; Umit Akbey3; Niels Chr. Nielsen1; 1Interdisciplinary Nanoscience

Center, Aarhus University, Aarhus, Denmark; 2Leibniz-Institut fuer Molekulare Pharmakologie, Berlin, Germany; 3Berliner

Sparkesse, Berlin, Germany In biological solid-state NMR an increasing interest in extensively deuterated samples is observed, as a means to dilute the strongly coupled protons. We present novel applications for the interleaved sampling strategy named RAPID (Relaxation-optimized Acquisition of Proton Interleaved with Deuterium) that for such samples takes advantage of polarization originating from both protons and deuterons, as a source to e.g. 13C spectra, instead of using only polarization on one of the spin species. It takes advantage of the highly different relaxation rates for 1H and 2H and the outcome is increased spectral information content per time unit or sensitivity enhancement. We extend the principles of interleaved sampling to various applications involving different combinations of nuclei and direct/indirect detection protocols.

Poster 366

Membrane Location Studies of HIV gp41 Constructs by 13C – 2H REDOR

Li Xie; David Weliky; Michigan State University, East Lansing, MI

HIV is a type of retrovirus that causes AIDS. A key step of HIV infection is the host cell-virus membrane fusion induced by HIV gp41 protein. Our group use Rotational Echo Double



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Resonance(REDOR) Solid State NMR to study HIV gp41 constructs such as HIV fusion peptide to correlate their membrane locations with fusion activities. Recently, we are developing a new REDOR method, 13C-2H REDOR, where one or several residues in the HIV gp41 construct is/are 13CO labeled, while the lipids are 2H labeled. Unlike 13C-31P REDOR and 13C-15N REDOR which apply 31P and 15N π pulses to reintroduce dipolar couplings, 13C-2H REDOR applies 2H π/2 pulses, which provides higher dephasing than applying 2H π pulses.

Poster 367

Fast and Ultra-fast MAS 13C-13C Correlations Applied to Biological Systems

Jean Paul Amoureux1; Olivier Lafon1; Julien Trebosc1; Bingwen Hu2; Gael de Paepe3; Qun Chen2; Ming Chen2;

Philippe Corcos1; 1Lille university, Villeneuve D'ascq, France; 2ECNU, Shanghai Key Laboratory of Magnetic Resonanc,

Shanghai, China; 3CEA/INAC, Grenoble, France When analyzing proteins, the assignment of 13C resonances must first be done. DQ-SQ experiments present the advantages of observing only one-bond correlations, short recoupling times, and no uninformative diagonal-peaks. We present H-BR2, which requires low rf-power, is robust to shielding and very simple to optimize, works at ultra-fast MAS, and does not require 1H decoupling. We demonstrate this sequence on YajG, a 192 amino acids protein. Then, long range correlations provide constraints to get the protein structure and folding. We present a new sequence, SHANGHAI, inspired by PARISxy the most broadband sequence currently. To decrease the experimental time, we use a covariance treatment which does not introduce uninformative diagonal peaks and use of non-uniform indirect sampling.

Poster 368 High-Resolution Proton CRAMPS NMR using Narrowband

Audio Filters and Postponed Sampling Donghua H. Zhou; Oklahoma State University, Stillwater, OK

Even with the fastest MAS probes the narrowest proton linewidths can only be obtained by using the combined rotation and multiple pulse spectroscopy (CRAMPS) method for fully protonated samples. Direct observation under windowed CRAMPS typically introduces 10-20 times more noise, partly because wideband audio filters have to be used or bypassed. Here we report utilization of narrowband filters in CRAMPS by taking advantage of the delay caused by the filters, which coincides with typical CRAMPS cycle times, enabling acquisition of the data in the next detection window. The noise of such spectra is about 5 times of MAS spectra. This new method allows CRAMPS to be performed on systems lacking wideline modules, such as spectrometers originally intended for solution NMR.

Poster 369

MAT, PASS or MATPASS? CPMG Sensitivity-enhanced Sideband Separation Experiment for

Disordered Solids with Large Anisotropy Ivan Hung1; Derrick Kaseman2; Sabyasachi Sen2; Zhehong

Gan1; 1National High Magnetic Field Laboratory, Tallahassee, FL; 2UC Davis, Davis, CA

A MATPASS/CPMG experiment is proposed for spinning sideband separation with enhanced sensitivity. The use of

MATPASS with CPMG gains an additional √2 in sensitivity over PASS/CPMG. The MATPASS/CPMG experiment is applied to GexSe4-x glasses which exhibit 77Se CSA and isotropic line widths over hundreds of kHz, beyond the fastest MAS rates currently available. The sideband separation allows for isotropic spectra and resolved spinning sidebands for CSA measurement. The use of CPMG multiple-echo acquisition enhances the signal-to-noise by an order of magnitude.

Poster 370

Use of Wideband Adiabatic Frequency Sweeps to Acquire Solid-state 195Pt NMR Spectra of Complicated

Heterogeneous Materials Louis Jones; Brad Chmelka; University of California, Santa

Barbara, Santa Barbara, CA Wideband uniform-rate smooth truncation (WURST-CPMG) pulses can be applied to probe local 195Pt environments in bulk and nanoscale solids. Improved signal resolution and sensitivity enable the observation of previously unobserved 195Pt environments. For example, 195Pt species in α-PtO2 are similar to surface oxides of Pt Black. Analogous solid-state 195Pt NMR measurements of PtS2reveal more disordered and shielded 195Pt environments, with lineshapes that are similar to reduced or sulfided Pt Black. Oxidized or sulfided Pt nanoparticles supported on SiO2, Al2O3, or NaY zeolite exhibit 195Pt lineshapes that reflect distinct oxidic or sulfided 195Pt species. Adiabatic excitation of large frequency ranges allows NMR spectra with ultrabroad signals to be acquired, the benefits and future prospects of which will be highlighted.

Poster 371

Broadband Excitation in MAS NMR of I = 1/2 Spins in Paramagnetic Systems with DANTE Echoes

Diego Carnevale1; Veronika Vitzthum1; Olivier Lafon2; Julien Trébosc2; Jean-Paul Amoureux2; Geoffrey Bodenhausen1, 3;

1EPFL, Lausanne, Switzerland; 2UCCS, CNRS 8181, Université de Lille, Villeneuve d'Ascq, France; 3Ecole Normale

Supérieure, Paris, France DANTE schemes prove extremely useful in site-selective excitation in the ultra-fast MAS regime. We demonstrate the efficiency of DANTE in 19F MAS NMR of CeF3, where the paramagnetic interaction causes the fluorine MAS spectrum to be characterized by inhomogeneous broadening of the order of 1 MHz. A spin-echo in which both excitation and refocusing steps are performed with DANTE proves extremely efficient in yielding an undistorted spectrum. The proposed method achieves uniform excitation at weak rf field strengths on the order of 30 kHz. We also demonstrate that delays alternating with nutation can yield a broadband Ԉ rotation over the entire manifold of spinning sidebands.

Poster 372

Spin-Lattice Relaxation Time-Constant Distributions of Heterogeneous Samples Used as Models for Shale

Rex Gerald; Lingyu Chi; Klaus Woelk; Missouri University of Science and Technology, Rolla, MO

NMR measurements are used to quantify content and microscopic distribution of oil in shale samples to estimate the value of shale fields. We have reconfigured a Varian Inova 400-MHz spectrometer to operate with a Bruker MiniSpec 20-MHz magnet to acquire nuclear spin relaxation data at low field. Control experiments were performed with a series of



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samples in 5-mm NMR tubes. The tubes contained water-sand mixtures doped with a relaxation agent and were characterized by single T1 time constants. Different combinations of up to nine control sample tubes were inserted in the low-field NMR probe. Complex inversion-recovery curves were fitted to a discrete sum of exponential terms. By combining different numbers and kinds of control samples, various bimodal distributions were mimicked.

Poster 373

Residual Dipolar Coupling Measurements in Solid-State NMR

Pierre Thureau; Institut de Chimie Radicalaire, Marseille, France

In solid-state NMR, the measurement of long-range dipolar couplings remains difficult in the case where the sample contains clusters of many magnetic nuclei. Inspired by solution-state NMR where residual dipolar couplings (RDCs) are currently used for structure determination, we show here that RDCs measurements can be transferred to solid-state NMR for the measurements of long-range dipolar couplings in multiple-spin coupled networks. The presented methodology has been used in uniformly 13C-labelled powder samples to measure dipolar couplings between 13C nuclei separated by distances exceeding 600 picometers. Furthermore, this methodology will be illustrated for 1H-1H distance measurements in natural abundance isotopic samples. In this latter case, dipolar couplings between 1H nuclei separated by distances exceeding 350 picometers have been measured.

Poster 374

Broadband Solid-state MAS NMR Spectroscopy of Paramagnetic Lithium Transition Metal Phosphate

Materials Andrew Pell1; Raphaele J. Clement1, 2; Ben Zhou2; Fiona

Strobridge2; Derek S. Middlemiss2; Lyndon Emsley1; Clare P. Grey2; Guido Pintacuda1; 1ENS Lyon, Villeurbanne, France;

2University of Cambridge, Cambridge, UK We present a 31P/7Li MAS-NMR study aimed at the structure characterization of a family of paramagnetic LiTMPO4 compounds with different ratios of Mn(II) to Fe(II) ions, which are promising candidates for new Li-ion cathode materials. The Fermi contact and dipolar interactions between the unpaired electrons and nuclear species result in very large shifts and shift anisotropies which contain potentially useful information. However they also make broadband excitation extremely difficult, and result in extensive overlap between the sideband patterns due to different sites. These problems can be solved by using short high-power adiabatic pulses (SHAPs), and incorporating them in a MAT-type sequence under ultra-fast MAS to separate the overlapping resonances giving highly-resolved spectra, that we assigned and interpreted using DFT methods.

Poster 375

Probing Dynamical Changes in Elastomers Induced by Magic Angle Spinning

Odingo Mitchell1; Cheng Sun2, 2; Gregory Boutis1, 1; 1Brooklyn College Physics Department, Brooklyn, NY; 2Dalian Institute

of Chemical Physics, Dalian, China The centripetal force on the sample caused by high spinning frequencies in MAS NMR will produce a strain which is known to cause noticeable effects on microscopic structure. In this

work we investigate the 13C T1ρ relaxation times to study induced dynamical changes on natural rubber due to sample spinning. The experimental values of the T1ρ times are used to extrapolate the correlation times which represent the fluctuating dipolar fields experienced by the 13C spins, pertaining to the overall motions of the carbon nucleus and neighboring protons. Our results demonstrate that the overall carbon correlation times decrease with increasing the spinning frequency as expected, based on simple entropy arguments, while the 13C chemical shifts appear to not vary significantly.

Poster 376

Average Hamiltonian Analysis of Pulse Errors in an Eight Pulse-Spin Counting Experiment

Yelena Zelenova; Steven Morgan; Gregory Boutis; Brooklyn College/CUNY, Brooklyn , NY

Spin counting NMR is a well known experimental technique that allows for determining the size and time evolution of networks of dipolar coupled nuclear spins. The method typically involves implementing an eight-pulse multiple pulse sequence whose effective Hamiltonian, to zeroth order of the Magnus expansion, is the double quantum Hamiltonian. In this work, we report on an average Hamiltonian treatment of pulse errors i.e. phase transients, phase errors and finite pulse width artifacts, as well as offset effects. Our analysis demonstrates that only pulse flip errors and phase errors and contribute to the zeroth and first order terms of the Magnus expansion respectively and may significantly modify the many-body spin dynamics under the multiple pulse sequence.

Poster 377

New Insights in High Resolution Solid-State Proton NMR & Proton Chemical Shifts for Powder Crystallography

Meghan Halse1; Maria Baias1; Jean-Nicolas Dumez1; Graeme Day2; Lyndon Emsley1; 1ENS Lyon, Lyon, France; 2University

of Cambridge, Cambridge, England First, with the objective of establishing a protocol for natural abundance NMR crystallography for crystal structure elucidation of powdered solids we demonstrate the possibility of complete ab initio structure determination in molecular crystals using combined 1H NMR and computationally based structure prediction techniques. Second, one of the barriers to further progress with this approach is the possibility to measure proton chemical shifts in powders. Towards this end we will present our most recent progress with homonuclear dipolar decoupling strategies. Notably, we will introduce a new parameterisation scheme for eDUMBO type decoupling, we will provide a framework which covers both PMLG and DUMBO decoupling, and we will explore the differences and similarities of the two schemes.

Poster 378 Optimizing Nanotube Diameter for Aligning Lipid Bilayers

and Membrane Proteins for Structure-function Studies by ssNMR

Alexander A. Nevzorov; Antonin Marek; Wenxing Tang; Alex I. Smirnov; North Carolina State University, Raleigh, NC

We report on further progress in developing nanotube supported lipid arrays as versatile bilayer mimetics for structure-function studies of membrane proteins by ssNMR. A series of homogeneous and hexagonally ordered nanoporous anodic aluminum oxide (AAO) substrates with different pore



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diameters were fabricated and employed for aligning lipid bilayers composed from DOPC/DOPG (9:1 molar ratio) lipids and 10 mol% of uniformly labeled Pf1 coat protein. The 80 nm substrates demonstrated exceptional superior macroscopic and signal-to-noise ratio for 2D ssNMR spectra.

Poster 379

R3-INEPT for Alumino-Phosphates Revisited : Efficiency and B1 Robustness

Julien Trebosc1; Olivier Lafon1; Francis Taulelle2; Charlotte Martineau2; Jean Paul Amoureux1; 1UCCS-CNRS UMR8181-

Univ Lille1, Villeneuve D'ascq Cedex, France; 2Institut Lavoisier de Versailles (ILV), Versailles, France

In 2007, we introduced different dipolar based INEPT sequences using R3 re-coupling. Magnetization is transferred from a quadrupolar spin to a spin ½ sending a dipolar re-coupling on the spin ½ only for best magnetization control. Here we give a detailed analysis of the properties of the different versions. The effect of CSA and B1 robustness is demonstrated experimentally on Alumino-phosphates and analyzed using simulations. Finally, we present a high resolution version MQ-R3-INEPT where a MQMAS filter removes the 2nd order quadrupolar broadening in F1 dimension. Signal is maximized using echo and anti-echo in a split-t1 pathway in addition to SPAM technique. Results on different AlPOs are shown.

Poster 380

Spin Counting and Decoherence during Dipolar Evolution in Liquid Crystal MBBA

Ana Karina Chattah1, 2; Agustín Gomez1; Horacio Pastawski1,2; Patricia Levstein1, 2; 1FaMAF, Córdoba,

Argentina; 2IFEG-CONICET, Córdoba, Argentina In this work we present multiple quantum solid state NMR experiments to study the many-body proton dynamics in liquid crystal MBBA. A pulse sequence involving evolution, mixing and detection is used, where the dynamics is governed by the dipolar Hamiltonian (H0

xx) during a time t. Initially the system is in equilibrium with the Zeeman field and a rotation around the z axis encodes the multiple quantum coherence orders. A spin-lock field applied during mixing (2t1) generates the reverted dynamics (– H0

xx/2). By measuring the Loschmidt Echo (LE) after H0

xx and – H0xx, information on the intrinsic

decoherence of the system is obtained. Comparison between Les resulting from local or global initial conditions are discussed.

Poster 381

Measurement of Chemical Shift Anisotropy for the Backbone Sites of U-13C, 15N-enriched Proteins via CSA

Amplification Ivan Hung1; Xiaoli Liu2; Mali Liu2; Conggang Li2; Zhehong

Gan1; 1National High Magnetic Field Laboratory, Tallahassee, FL; 2Wuhan Institute of Physics and Mathematics,

Wuhan, China Extended chemical shift amplification (XCSA) is applied for measuring CSA in uniformly labeled proteins. XCSA is a constant-time experiment with π-pulses during which the CSA is amplified while the 13C-13C homonuclear dipolar interaction remains averaged. 3D XCSA experiments with 15N-13C correlation allow site resolution for measuring backbone CSA as demonstrated using GB1.

SOLIDS: SMALL MOLECULES, 382 - 389

Poster 382 Study of HD and VX on Activated Carbon

William Creasy1; David McGarvey2; Roderick Fry2; 1SAIC, Aberdeen Proving Ground, MD; 2R&T Directorate, Edgewood

Chemical Biological Cent, Aberdeen Proving Ground, MD Adsorption of HD and VX on carbon materials was studied to determine whether chemical weapons agent is reactively decontaminated. VX was studied using P-31 High Resolution Magic Angle Spinning Nuclear Magnetic Resonance (HRMAS NMR), and C-13 labeled HD was studied by C-13 HRMAS NMR. Agents were added by pipeting 1 µl liquid drops on 10-20 mg of carbon powder, or using dilute solutions. Several different effects were observed. The NMR lines broadened over minutes to days of time, indicating that the agent was immobilized on the surface. Solvent was added, and some signal was recovered as narrow lines. VX hydrolyzed to products. The same carbon samples were thermally desorbed by headspace GC/MS, but only small fractions were recovered.

Poster 383

Measurement of Selective Multiple JCC Couplings in Small Molecules by Solid State NMR

Veera Mohan Rao K ; Jagadeesh Bharatam; Centre for NMR, Indian Institute of Chemical Techn, Hyderabad, India

1D Spin-echo modulation technique reported by Levitt, Brown and Co-workers for the determination of selective one-bond JCC couplings and the corresponding RDCs at MAS and off-MAS, respectively, has offered new basis for the development NMR-Crystallography of small molecules. However, the exercise of simultaneous measurement of multiple spin-couplings is challenging. We will discuss the experimental methods developed in our laboratory for simultaneous measurements of multiple one-bond and three-bond JCC couplings, for uniformly 13C-labeled small molecules. Furthermore, the accurate determination of J values could be accomplished by appropriate scaling methods, which showed excellent correlation with those obtained in solution state. We also briefly discuss our results on the determination of RDCs and inter-nuclear distances in these molecules.

Poster 384 Solid-State NMR Structural Analysis of Self-Assembling

Designer Peptides RADA16-I and MAX8 Sarah Leonard1, 2; Ashley Cormier1, 2; Max Zimmerman1; Xiaodong Pang1; Huan-Xiang Zhou1; Anant Paravastu1, 2;

1The Florida State University, Tallahassee, FL; 2National High Magnetic Field Laboratory, Tallahassee, FL

The peptides RADA16-I and MAX8 each possess amino acid sequences chosen rationally to self-assemble into β-sheet nanofiber networks. Solid state NMR spectroscopy was used on selectively 13C labeled samples to probe nanofiber molecular structure. NMR measurements included 1H-13C CPMAS, 2D exchange via fpRFDR recoupling, and PITHIRDS-CT. For RADA16-I nanofibers, NMR data indicate linear β-strands. PITHIRDS-CT data constrain schemes for inter-molecular organization. MAX8 nanofibers were analyzed using a combination of natural abundance 1H-13C CPMAS and PITHIRDS-CT experiments with selective carbonyl 13C labels. Lack of strong 13C-13C dipolar couplings contradicts molecular structures proposed in the literature. We will discuss structural



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models for RADA16-I and MAX8 nanofibers and how these results impact rational design of self-assembling peptides.

Poster 385

Thermodynamic Isotope Effects in the NMR Spectra of Partially Deuterated Amino Acids

Monica Kinde; Jun Zhou; Gerard Harbison; University of Nebraska-Lincoln, Lincoln, NE

A common assumption in NMR is that isotope labeling is not perturbative. This is often not so for deuterium. Theory and experiment demonstrate that fully deuterated (–ND3

+) and partially deuterated (–NDH2

+) amino groups in three distinct crystalline amino acids have substantially different 2H spectra, because of partitioning of deuterium out of strong hydrogen bonds, which disrupts averaging by thermally activated hops of the group. Thermochemical quantum calculations allow us to compute deuterium partitioning between the three sites, and reproduce the effect. Such computations predict similar but somewhat smaller effects in partially deuterated methyls, particularly if one site is sterically crowded. Accurate computation of methyl and amino group spectra and spin relaxation requires accounting for these effects.

Poster 386

Measuring Packing Interactions in the Antibiotic Ciprofloxacin: A Combined Solid-state NMR, X-ray

Diffraction and Computer Simulation Study Luís Mafra1, 2; Sérgio Santos1; Renée Siegel1; Inês Alves1; Filipe Paz1; Dmitri Dudenko2; Hans Spiess2; 1University of

Aveiro, Aveiro, Portugal; 2Max-Planck-Institut für Polymerforschung, Mainz, Germany

We present an experimental NMR, X-ray diffraction (XRD), and computational study of the supramolecular assemblies of two crystalline forms of Ciprofloxacin: one anhydrate and one hydrate forming water wormholes. The resonance assignment of up to 51 and 54 distinct 13C and 1H resonances for the hydrate is reported. The effect of crystal packing on the 1H and 13C chemical shifts including weak interionic H-bonds, is quantified; 1H chemical shift changes up to ~-3.5 ppm for CH···pi contacts and ~+2 ppm (CH···O (-)); ~+4.7 ppm (

(+)NH···O (-)) for H- bonds. Water intake induces chemical shift changes up to 2 and 5 ppm for 1H and 13C nuclei, respectively. Such chemical shifts are found to be sensitive detectors of hydration/dehydration in highly insoluble hydrates.

Poster 387

Understanding Relaxation in Solid Pharmaceutical Formulations: Causes, Uses, and Ways to Overcome

Long Relaxation Times Eric Munson1; Elodie Dempah1, 2; Dewey H. Barich2; Benjamin N. Nelson2; Joseph Lubach2; Loren Schieber2; David Lewis3;

John Heinrich3; 1University of Kentucky, Lexington, KY; 2University of Kansas, Lawrence, KS; 3Revolution NMR LLC,

Fort Collins, CO Relaxation times, specifically 1H T1 relaxation times, can be quite long in crystalline pharmaceutical solids. This plays a critical role in the acquisition of CPMAS NMR spectra of drug formulations. The most common relaxation sinks for these compounds are either the surface of the crystal or a crystal defect. When the crystals have no defects, we have found that the particle size of the drug compounds can be correlated

back to the NMR relaxation time. When crystal defects are introduced in gabapentin, we have found that relaxation times correlate well with chemical degradation rates of gabapentin to the lactam. Finally, an update to our new probe technology that helps to overcome the down side of long relaxation times is presented.

Poster 388

Multinuclear Solid-state MAS NMR Techniques and Computational Methods for the Assignment of Small

Molecules Mariana Sardo1; Renée Siegel1; Sérgio M. Santos1; João

Rocha1; José R. B. Gomes1; Luis Mafra1, 2; 1CICECO, Chemistry Department -University of Aveiro, Aveiro, Portugal;

2Universidad de Oviedo, Oviedo, Spain This contribution focuses on the complete NMR assignment of powdered tripeptide glutathione at natural isotopic abundance, based on J-coupling and dipolar NMR techniques combined with 1H CRAMPS decoupling. Our work illustrates how multiple 2D high-resolution solid-state NMR methods, such as 1H-13C INEPT-HSQC, 1H-13C PRESTO-HETCOR, 1H-1H double-quantum and 1H-14N D-HMQC correlation experiments, combine with chemical shift calculations to fully assign a variety of functional groups. To support the experimental data, two different codes (CASTEP and Quantum ESPRESSO) are compared and tested for the calculation of 1H and 13C chemical shifts.

Poster 389

Solid-state NMR Based Structural Characterization of Oligomeric Amyloid-β (1-42) Peptide

Danting Huang1, 3; William Tay2; Terrone Rosenberry2; Anant Paravastu1, 3; 1Florida State University, Tallahassee, FL;

2Mayo Clinic Jacksonville, Jacksonville, FL; 3National High Magnetic Field Laboratory, Tallahassee, FL

We will present solid state NMR results on Aβ42 oligomers which indicate structural features which are inconsistent from previous Aβ42 oligomers models. Specifically, a 2D-fpRFDR spectrum from Aβ42 oligomers (~150 kDa or ~30-mers) isotopically labeled with uniform 13C and 15N at seven selective sites indicates a well-defined Aβ42 oligomer molecular structure with most signals consistent with β-strand secondary structure. The 2D RAD experiments applied to the same sample and a second isotopically diluted sample show that there is an inter-molecular interaction between F19 sidechain and A30/I31 sidechains. The PITHIRDS-CT experiments on Aβ42 oligomers which were selectively labeled at specific methyl carbon and carbonyl carbon sites indicate that, unlike with fibrillar states, molecules are not arranged as in-register parallel β-sheets.

POSTERS OF CONTRIBUTED TALKS, 390 - 412

Poster 390 Structure and Dynamics of a Microcrystalline

Metalloprotein by Solid-state NMR : Proton-detection, Ultra-fast MAS and Paramagnetic Restraints; Michael J.

Knight1; Andrew Pell1; Ivano Bertini2; Isabella C. Felli2; Leonardo Gonnelli2; Roberta Pierattelli2; Torsten Herrmann1;

Lyndon Emsley1; Guido Pintacuda1; 1ENS-Lyon, Villeurbanne, France; 2CERM - University of Florence, Florence, Italy



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Poster 391 Protein Fold Determined by Paramagnetic Magic-Angle

Spinning Solid-State NMR Spectroscopy; Ishita Sengupta; Ohio State University, Columbus, OH

Poster 392

Design Considerations for High-Temperature-Superconducting NMR Probes; Vijaykumar Ramaswamy1;

Jerris Hooker2; Richard Withers3; Robert Nast3; William Brey2; Arthur Edison1, 2; 1University of Florida, Gainesville, FL; 2National High Magnetic Field Lab, Tallahassee, FL; 3Agilent

Technologies, Santa Clara, CA

Poster 393 Compressed Sensing Reconstruction of Undersampled

NOESY Spectra: Application to Large Membrane Proteins; Mark Bostock1; Daniel Holland2; Daniel

Nietlispach1; 1Department of Biochemistry, University of Cambridge, United Kingdom; 2Magnetic Resonance Research

Centre, University of Cambridge, United Kingdom

Poster 394 NMR Detection of Redox Reactions in Cu2+-Bound

Amyloid-β Fibrils and Resolution Enhanced Solid-State NMR by SAIL and Ultra Fast MAS; Sudhakar

Parthasarathy1; Yusuke Nishiyama2; Yuki Endo2; Takahiro Nemoto2; Masatsune Kainosho3, 4; Yoshitaka Ishii1; 1Univ. of

Illinois at chicago, Chicago, IL; 2JEOL Ltd., Tokyo, Japan; 3Graduate School of Science, Nagoya University, Nagoya, Japan; 4Center of Priority Areas, Tokyo Metropolitan Univ,

Tokyo, Japan

Poster 395 Analysis Pipeline for Simultaneous Study of Structure and Dynamics of Challenging Proteins from Residual

Dipolar Couplings; Stephanie Irausquin; Christopher Schmidt; Mikhail Simin; Homayoun Valafar; University of

South Carolina, Columbia, SC

Poster 396 Model of Large Scale Conformation Mobility in Proteins; Yaroslav Ryabov1; G. Marius Clore2; Charles D. Schwieters1; 1DCB, CIT, NIH, Bethesda, MD; 2NIDDK, NIH, Bethesda, MD

Poster 397

Generating MRI Contrasts in Rotating Frames of Rank 1≤n≤5 in the Human Brain at 4T and Mouse Brain at 7T;

Timo Liimatainen1; Silvia Mangia2; Hanne Hakkarainen1; Andrew Tyan2; Djaudat Idiyatullin2; Dennis Sorce2; Michael Garwood2; Shalom Michaeli2; 1University of Eastern Finland,

Kuopio, Finland; 2CMRR, University of Minnesota, Minneapolis, MN

Poster 398

Fast Reconstruction of 0.8% Non-Uniformly Sampled 4D Methyl-Methyl NOESY by Iterative Soft Thresholding;

Sven G. Hyberts; Alexander G. Milbradt; Gerhard Wagner; Dept. Biol. Chem. & Mol. Pharmacologie, Boston, MA

Poster 399

SUCCESS: Suppression of Undesired Chemicals using Contrast-Enhancing Singlet States; Stephen Devience1;

Ronald Walsworth2, 3; Matthew Rosen4, 5; 1Harvard University

Department of Chemistry and Che, Cambridge, MA; 2Harvard-Smithsonian Center for Astrophysics, Cambridge, MA;

3Harvard University Department of Physics, Cambridge, MA; 4Harvard Medical School, Boston, MA; 5Martinos Center for

Biomedical Imaging, Boston, MA

Poster 400 High-Pressure NMR Reveals that the Native State of

Proteins Contains the "Dry" Molten Globule; Yinan Fu1; Vignesh Kasinath1; Veronica Moorman1; Nathaniel Nucci1;

Vincent Hilser2; Joshua Wand1; 1Univ of Pennsylvania, Philadelphia, PA; 2Johns Hopkins University, Baltimaore, MD

Poster 401

2D Ultrafast J-resolved MRS Sequence with 3D Localization: an in vitro Validation on a 7T Imaging

System; Serge Akoka1; Tangui Roussel2; Patrick Giraudeau1; Hélène Ratiney2; Sophie Cavassila2; 1CEISAM, UMR 6230, CNRS/Université de Nantes, Nantes, France; 2CREATIS,

UMR 5220, Universite de Lyon, Lyon, France

Poster 402 In-situ 7Li MRI of Li-ion Batteries; S. Chandrashekar1;

Nicole Trease2; Hee-Jung Chang2; Alexej Jerschow1; Clare P. Grey3; 1new york university, New York, NY; 2stony brook

university, stony brook, NY; 3University of Cambridge, Cambridge, United Kingdom

Poster 403

Automating the Processing and Analysis of High Throughput Ligand-Protein Binding Spectra within the MestReNova System; Chen Peng1; Manuel Perez1; Juan

Carlos Cobas1; Xiaolu Zhang2; Jasna Fejzo2; Jaison Jacob2; Andreas Lingel3; 1Mestrelab Research, Santiago de

Compostela, Spain; 2Novartis Institutes for BioMedical Research, Inc., Cambridge, MA; 3Novartis Institutes for

Biomedical Research, Emeryville, CA

Poster 404 Metabolomics of Intact Tissues: Discrimination Between

Different Regions of Osteolytic Lesions in Multiple Myeloma Patient using 1H HRMAS NMR spectra; Silvia

Mari1, 4; Francesca Fontana1; Jose Garcia Manteiga1; Edoardo Gaude1; Simone Cenci1; Enrico Caneva2; Giovanna Musco1; Stanislav Sykora3; Juan Carlos Cobas Gomez5; 1S. Raffaele Scientific Institute, Milan, IT; 2Università degli Studi di Milano, Milan, IT; 3Extra Byte, Castano Primo, IT; 4R4R, Rodano, IT;

5Mestrelab Research, Santiago de Compostela, ES

Poster 405 Boosting Sensitivity of Ligand-Protein Screening by NMR of Long-Lived States; Nicola Salvi; Aurélien Bornet; Roberto

Buratto; Geoffrey Bodenhausen; Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland

Poster 406

Supramolecular Structure of Membrane-Associated Polypeptides by Combining Solid-State NMR and

Molecular Dynamics Simulations; Markus Weingarth1; Christian Ader1; Adrien Melquiond1; Deepak Nand1; Olaf

Pongs2; Stefan Becker3; Alexandre M. J. J. Bonvin1; Marc Baldus1; 1Utrecht University, Bijvoet Center, Utrecht,

Netherlands; 2Instut fur Neurale Singnalverabeitung,Univ



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Hamburg, Hamburg, Germany; 3Max Planck Insitute for Biophysical Chemistry, Gottingen, Germany

Poster 407

Dual Acquisition Magic Angle Spinning (DUMAS) Solid-State NMR: A New Approach to Simultaneous Acquisition

of Multi Dimensional Spectra of Biomacromolecules; Gopinath Tata1, 2; Gianluigi Veglia1, 2; 1University of

Minnesota, Minneapolis, MN; 2University of Minnesota, Minneapolis, MN

Poster 408

High Spin-Lock (> 4 kHz) for R1rho using a Cryogenically Cooled Probe.; David Ban1; Alvar Gossert2; Helena Kovacs3; Karin Giller1; Stefan Becker1; Christian Griesinger1; Donghan

Lee1; 1Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; 2Novartis Institutes of BioMedical

Research, Basel, Switzerland; 3Bruker BioSpin AG, Fällanden, Switzerland

Poster 409

Improved Knowledge-Based Torsion-Angle Potentials Yield Higher-Quality NMR Structures of Proteins; Guillermo A. Bermejo; G. Marius Clore; Charles D.

Schwieters; National Institutes of Health, Bethesda, MD

Poster 410

How to Measure the Performance of Automated Structure Verification Systems using Negative Control Structures; Gonzalo Hernández; Vis Magnetica, Montevideo, Uruguay

Poster 411

Magic Angle Spinning Dynamic Nuclear Polarization NMR at 700 MHz/460 GHz; Vladimir K. Michaelis1; Eugenio

Daviso1, 2; Evgeny Markhasin1; Alexander B. Barnes1; Emilio A. Nanni1; Sudheer K. Jawla1; Ajay Thakkar1; Ronald

DeRocher1; Judith Herzfeld2; Richard J. Temkin1; Robert G. Griffin1; 1Massachusetts Institute of Technology, Cambridge,

MA; 2Brandeis University, Waltham, MA

Poster 412 Paramagnetic Mapping of the 116 kDa

Ca2+ATPase/Phospholamban Membrane Protein Complex in Lipid Bilayers by Solid State NMR Spectroscopy; Martin

Gustavsson1; Raffaello Verardi1; Nathaniel J Traaseth2; Gianluigi Veglia1; 1University of Minnesota, Minneapolis, MN;

2New York University, New York, NY

INDEX OF AUTHORS

Program Code: M, T, W, Th, F = Day O = Oral Time Poster is followed by board space.

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Abraham, Anuji ............................ Poster 282 Acosta, Rodolfo Hector ........ThOE 4:00-4:25 Acosta, Victor ............................... Poster 124 Adams, Ralph W. ......................... Poster 202 Adelson, Charles N. ..................... Poster 238 Ader, Christian ................ ThOC 11:50-12:05 Adriany, Gregor ........................... Poster 119 Aguilar, Juan ................................ Poster 204 Aguilar, Juan A. ........................... Poster 202 Agustin Alvarez, Gonzalo WOB 12:05-12:20 Ahn, Jinwoo ................................. Poster 045 Ahn, Jinwoo ................................. Poster 040 Aihara, Yuichi ............................... Poster 094 Akbey, Umit .................... ThOC 11:35-11:50 Akbey, Umit ................................. Poster 365 Akel, Chris ................................... Poster 130 Akke, Mikael ......................... TOD 5:35-5:50 Akoka, Serge ....................... WOE 4:50-5:05 Al-Hashimi, Hashim ............. WOD 5:20-5:35 Al-Hashimi, Hashim ..................... Poster 112 Almeida, Fabio C. L. .................... Poster 050 Almeida, Fabio C. L. .................... Poster 041 Al-Mosawi, Maithan K. ..... WOC 12:05-12:20 Alves, Inês ................................... Poster 386 Ames, James B. ........................... Poster 263 Amoureux, Jean Paul .................. Poster 132 Amoureux, Jean Paul .................. Poster 268 Amoureux, Jean Paul .................. Poster 379 Amoureux, Jean Paul ........... MOD 5:05-5:20 Amoureux, Jean Paul .................. Poster 367 Amoureux, Jean-Paul .................. Poster 371 Anai, Takahiro .................... WOA 9:50-10:05 Andreas, Loren ................. MOB 12:05-12:20 Andreas, Loren ..................... MOD 4:50-5:05 Andrew, Brian .................. WOC 11:50-12:05 Andrew, Brian .............................. Poster 123 AnoBom, Cristiane ....................... Poster 192 Antusek, Andrej ........................... Poster 273 Arbogast, Luke ............................. Poster 194 Ardenkjær-Larsen, Jan H. .... WOE 5:35-5:50 Ardenkjær-Larsen, Jan H. ............ Poster 155 Ardenkjær-Larsen, Jan Henrik ..... Poster 158 Ardenkjaer-Larsen, Jan Henrik ............................................. WOA 9:20-9:30 Arey, Bruce W. ............................. Poster 344 Ariza-Castolo, Armando .......ThOE 5:35-5:50 Armstrong, Geoffrey S. ................ Poster 021 Arnold, Alexandre A. .................... Poster 002 Arnold, Alexandre A. .................... Poster 005 Arthanari, Haribabu ...................... Poster 196 Asano, Atsushi ............................. Poster 339 Asano, Atsushi ............................. Poster 239 Ashida, Jun .................................. Poster 306 Assadi-Porter, Fariba M. .............. Poster 059 Auccaise, Ruben ..................ThOE 4:25-4:50 Auclair, Karine ............................. Poster 108 Aussenac, Fabien ........................ Poster 132 Autschbach, Jochen .................... Poster 349 Avalos, Claudia ............................ Poster 124 Axe, Jennifer ........................ WOD 4:25-4:50 Azeredo Braga, Carolina ............. Poster 030 Bachmann, Brian ......................... Poster 095 Badilita, Vlad ......................... MOE 5:35-5:50 Bai, Yang ..................................... Poster 298 Baias, Maria ................................. Poster 377 Bain, Alex D. ................................ Poster 083 Bain, Alex D. ................................ Poster 118 Bajaj, Vikram ................................ Poster 124 Bajaj, Vikram ................................ Poster 325 Bajaj, Vikram S. .....................FOA 9:35-9:50 Bajaj, Vikram S. ........................... Poster 018

Bajaj, Vikram S. ........................... Poster 161 Baker, David ....................... ThOD 5:05-5:20 Bala, Lakshmi .............................. Poster 249 Balaceanu, Andreea Cristina ....... Poster 110 Balasubramaniam, Ambikaipakan ..................................................... Poster 248 Baldus, Marc ................... ThOC 11:50-12:05 Baldus, Marc ......................... FOA 8:55-9:20 Balsgart, Nicholas ........................ Poster 299 Baltisberger, Jay H. ..................... Poster 272 Baltisberger, Jay H. ..................... Poster 364 Baltisberger, Jay H. ..................... Poster 343 Ban, David .......................... ThOD 4:50-5:05 Bandosz, Teresa .......................... Poster 342 Bankhead III, Armand .................. Poster 246 Barbet-Massin, Emeline .. ThOC 11:35-11:50 Barcus, Scott ............................... Poster 147 Bardelang, David ......................... Poster 232 Barich, Dewey H. ......................... Poster 387 Barker, Jeffrey ............................. Poster 168 Barlow, Michael J. ....................... Poster 147 Barlow, Michael J. ....................... Poster 162 Barnes, Alexander ....................... Poster 180 Barnes, Alexander B. ................... Poster 188 Barnes, Alexander B. ........ FOB 11:50-12:05 Barrère, Caroline ......................... Poster 091 Bartoschek, Stefan .......... WOB 11:35-11:50 Basser, Peter J. .................. ThOA 9:20-9:35 Baum, Jean .................................. Poster 031 Bax, Ad ............................. MOB 11:10-11:35 Bayro, Marvin ............................... Poster 325 Bayro, Marvin J. ........................... Poster 266 Bazov, Emmanuel ........................ Poster 063 Beard, William .............................. Poster 010 Beaugrand, Maïwenn ................... Poster 002 Becker, Julia ................................ Poster 018 Becker, Stefan ................. WOB 11:35-11:50 Becker, Stefan ................ ThOC 11:50-12:05 Becker, Stefan .................... ThOD 4:50-5:05 Bednarek, Elzbieta ....................... Poster 019 Bednarek, Elzbieta ....................... Poster 217 Bednarek, Elzbieta ....................... Poster 020 Beduz, Carlo .................... WOC 12:05-12:20 Behnke, Thomas .......................... Poster 348 Belenky, Marina ........................... Poster 266 Bensky, Guy .................... WOB 12:05-12:20 Berlin, Konstantin ......................... Poster 070 Bermejo, Guillermo A. ......... ThOD 5:20-5:35 Bernstein, Michael ....................... Poster 304 Bernstein, Michael ....................... Poster 305 Bernstein, Michael ....................... Poster 302 Berthold, Deborah ........................ Poster 328 Berthold, Deborah ................. TOA 9:20-9:35 Bertin, Nadia ......................... MOE 4:50-5:05 Bertini, Ivano ..................... MOB 11:50-12:05 Bertini, Ivano ................................ Poster 127 Bertran, Celso A. ......................... Poster 333 Bezsonova, Irina .......................... Poster 061 Bharatam, Jagadeesh .................. Poster 383 Bharatam, Jagadeesh .................. Poster 218 Bhate, Manasi ................. ThOC 10:45-11:10 Bhattacharyya, Jaya .................... Poster 060 Billeter, Martin .............................. Poster 041 Bingol, Kerem .............................. Poster 244 Bjerring, Morten ........................... Poster 365 Blackburn, Mandy ........................ Poster 048 Blackburn, Mandy ........................ Poster 032 Blackledge, Martin .......... ThOC 11:35-11:50 Blommers, Marcel ............ WOB 11:35-11:50 Blus, Bartlomiej ............................ Poster 060 Bocian, Wojciech ......................... Poster 020

Bocian, Wojciech ......................... Poster 217 Bocian, Wojciech ......................... Poster 019 Bockmann, Anja ........................... Poster 335 Bockmann, Anja ........................... Poster 316 Bodenhausen, Geoffrey .. ThOB 12:02-12:20 Bodenhausen, Geoffrey ............... Poster 371 Bodenhausen, Geoffrey ....... WOA 8:55-9:20 Boehr, David ........................ WOD 4:25-4:50 Boettcher, John ............................ Poster 009 Boettcher, John ............................ Poster 330 Böhme, Ute .................................. Poster 235 Bonagamba, Tito J. ............. ThOE 4:25-4:50 Bonvin, Alexandre M. J. J.ThOC 11:50-12:05 Bornet, Aurélien ................... WOA 8:55-9:20 Bornet, Aurélien .............. ThOB 12:02-12:20 Borowicz, Piotr ............................. Poster 019 Bos, Martine .......................... FOA 8:55-9:20 Bostock, Mark ....................... TOA 9:35-9:50 Botana, Adolfo ............................. Poster 221 Botana, Adolfo ................. WOC 11:50-12:05 Botana, Adolfo ............................. Poster 207 Bouchard, Jill ............................... Poster 255 Bouchevreau, Boris...................... Poster 268 Boudreau, Eilis ............................. Poster 246 Bousset, Luc ................................ Poster 316 Boutin, Celine ............................... Poster 163 Boutis, Gregory ............................ Poster 063 Boutis, Gregory ............................ Poster 121 Boutis, Gregory ............................ Poster 375 Boutis, Gregory ............................ Poster 376 Bowen, Sean ................................ Poster 131 Bowen, Sean ................................ Poster 158 Bowers, Clifford R. ....................... Poster 109 Bowers, Clifford R. ....................... Poster 130 Bozkurt, Neslihan ......................... Poster 276 Bradley, Scott ................... WOB 11:10-11:35 Branca, Rosa Tamara .................. Poster 117 Brey, William ................................ Poster 040 Brey, William ......................... MOE 5:05-5:20 Brey, William W. ........................... Poster 179 Brey, William W. ........................... Poster 185 Brey, William W. ........................... Poster 215 Brey, William W. ........................... Poster 177 Brieba-de-Castro, Luis ................. Poster 067 Brothers, Michael ......................... Poster 008 Brown, Douglas E. ....................... Poster 289 Brown, Leonid .............................. Poster 334 Brown, Leonid .............................. Poster 332 Brown, Lynda J. ................... WOA 9:20-9:30 Brown, Richard C. D. ........... WOA 9:20-9:30 Brown, Truman R. ........................ Poster 098 Brubaker, William ......................... Poster 004 Bruschweiler, Rafael .................... Poster 244 Bruschweiler-Li, Lei ...................... Poster 244 Buck, Janina ........................ WOD 4:00-4:25 Budker, Dmitry ............................. Poster 124 Budker, Dmitry ...................... FOA 9:35-9:50 Buljubasich, Lisandro ........... WOA 8:30-8:55 Bulte, Jeff .............................. TOE 5:05-5:20 Buratto, Roberto .............. ThOB 12:02-12:20 Bureau, Bruno .............................. Poster 347 Burmistrov, Evgeny ...................... Poster 087 Burmistrov, Evgeny ...................... Poster 086 Burns, Brian ................................. Poster 164 Burton, Sarah ............................... Poster 040 Burton, Sarah ............................... Poster 114 Burum, Alex ................................. Poster 269 Butler, Mark .................................. Poster 124 Byeon, Chang-Hyeock ................. Poster 045 Byeon, In-Ja ................................. Poster 045 Byeon, In-Ja ................................. Poster 040

INDEX OF AUTHORS


Page 112

Byrd, R. Andrew ........................... Poster 190 Cabeça, Luis Fernando ............... Poster 116 Cabeça, Luis Fernando ............... Poster 120 Cady, Sarah D. ............................ Poster 319 Cady, Sarah D. ............................ Poster 320 Caldarelli, Stefano ....................... Poster 241 Canary, James ...................... MOE 5:20-5:35 Caneva, Enrico ................ThOB 11:50-12:05 Cano-Sánchez, Patricia ............... Poster 067 Caporini, Marc ............................. Poster 325 Carignani, Elisa ................ WOC 12:05-12:20 Carlomagno, Teresa ........ WOB 11:35-11:50 Carnevale, Diego ......................... Poster 371 Carosio, Maria Gabriela Aparecida ..................................................... Poster 122 Carravetta, Marina ........... WOC 12:05-12:20 Carter, Carol ......................... TOD 5:05-5:20 Caruso, Anthony .......................... Poster 352 Casabianca, Leah ........................ Poster 228 Casagrande, Fabio ...................... Poster 284 Casano, Gilles ............................. Poster 148 Cassani, Julia .............................. Poster 208 Cassani, Julia .............................. Poster 204 Cavagnero, Silvia ......................... Poster 151 Cavassila, Sophie ................ WOE 4:50-5:05 Celik, Ayhan ................................. Poster 276 Cenci, Simone .................ThOB 11:50-12:05 Chan, Kannie .........................TOE 5:05-5:20 Chandrana, Chaitanya ................. Poster 178 Chandrashekar, S. ...............ThOA 9:35-9:50 Chang, Hee-Jung .................ThOA 9:35-9:50 Chao, Fa-An ................................ Poster 066 Charrier, Benoît ........................... Poster 206 Chattah, Ana Karina ............ThOE 4:00-4:25 Chattah, Ana Karina .................... Poster 380 Chaudhari, Sachin ....................... Poster 233 Chauhan, Shyam S. ..................... Poster 293 Chaves, Luiz Artur ....................... Poster 192 Cheetham, Janet C. ..................... Poster 141 Chekmenev, Eduard .................... Poster 147 Chekmenev, Eduard .................... Poster 140 Chekmenev, Eduard .................... Poster 160 Chekmenev, Eduard .................... Poster 145 Chen, Der-Yow ............................ Poster 183 Chen, Fang .................................. Poster 077 Chen, Hsueh-Ying ....................... Poster 129 Chen, Hsueh-Ying ....................... Poster 131 Chen, Joseph ............................... Poster 240 Chen, Judy Y. .................. WOC 12:05-12:20 Chen, Kang ........................... TOD 5:05-5:20 Chen, Ming .................................. Poster 367 Chen, Qun ................................... Poster 367 Chen, Shizhen ............................. Poster 143 Chen, Song .................................. Poster 168 Chen, Wen ................................... Poster 057 Chen, Ying ................................... Poster 341 Chen, Yu-Hao ........................TOE 5:35-5:50 Cheng, Kun .................................. Poster 191 Cheng, Ren-Hao .......................... Poster 356 Cheng, Ren-Hao .......................... Poster 358 Cherry, Brian ................................ Poster 167 Chi, Lingyu ................................... Poster 225 Chi, Lingyu ................................... Poster 372 Chimon Peszek, Sandra .............. Poster 035 Chinthalapalli, Srinivas ........ WOA 8:55-9:20 Chmelka, Brad ............................. Poster 370 Chmelka, Brad .................. TOC 10:45-11:10 Cho, Gyunggoo ............................ Poster 090 Cho, Hyungjoon ........................... Poster 090 Cho, Junho .................................. Poster 248 Choi, In-Young ............................. Poster 169

Choi, In-Young ............................. Poster 170 Chou, James ..................... FOB 10:45-11:10 Chou, James ........................ MOD 4:50-5:05 Christen, Martin ........................... Poster 027 Christophe, Coperet ..................... Poster 148 Chun, Tang .................................. Poster 105 Ciobanu, Luisa ...................... TOE 4:50-5:05 Ciobanu, Luisa ............................. Poster 186 Clancy, Kate ................................ Poster 054 Clark, Lindsay ................... MOB 12:05-12:20 Clausen, Andrew M. .................... Poster 141 Clay, Mary .................................... Poster 009 Clement, Raphaele J. .................. Poster 374 Clore, G. Marius .................. ThOD 5:20-5:35 Clore, G. Marius .................... TOD 5:20-5:35 Clore, Marius .................... MOB 11:35-11:50 Cobas, Carlos .............................. Poster 302 Cobas, Carlos .............................. Poster 305 Cobas, Carlos .............................. Poster 304 Cobas, Juan Carlos ........ ThOB 11:35-11:50 Cobas Gomez, Juan Carlos ........................................ ThOB 11:50-12:05 Cobb, Justin ................................. Poster 225 Coffey, Aaron ............................... Poster 147 Coffey, Aaron ............................... Poster 145 Coffey, Aaron ............................... Poster 140 Cole, Jonathan ............................. Poster 261 Colnago, Luiz Alberto .................. Poster 122 Colnago, Luiz Alberto .................. Poster 116 Colnago, Luiz Alberto .................. Poster 120 Colson, Kimberly L. ...................... Poster 274 Columbus, Linda .......................... Poster 034 Comellas, Gemma ....................... Poster 328 Comment, Arnaud ........................ Poster 157 Communie, Guillaume .... ThOC 11:35-11:50 Concistre, Maria ............... WOC 12:05-12:20 Connors, Chris ............................. Poster 279 Conradi, Mark .............................. Poster 340 Constable, Todd .......................... Poster 258 Conzen, Suzanne ........................ Poster 205 Coote, Paul .................................. Poster 196 Corcos, Philippe ........................... Poster 347 Corcos, Philippe ........................... Poster 367 Cormier, Ashley ........................... Poster 384 Cornilescu, Claudia ...................... Poster 059 Cornilescu, Claudia C. ................. Poster 033 Cornilescu, Gabriel ...................... Poster 033 Cornilescu, Gabriel ...................... Poster 059 Corzilius, Bjorn ............................. Poster 144 Corzilius, Bjorn ............................. Poster 150 Corzilius, Bjorn ............................. Poster 127 Cote, Jacques .............................. Poster 058 Courtier-Murias, Denis ..... WOC 11:50-12:05 Courtier-Murias, Denis ................. Poster 247 Courtier-Murias, Denis ................. Poster 231 Courtier-Murias, Denis ................. Poster 123 Courtier-Murias, Denis ................. Poster 360 Courtney, Joseph ......................... Poster 328 Creasy, William ............................ Poster 210 Creasy, William ............................ Poster 382 Cross, R. Matthew ....................... Poster 285 Cross, Timothy ............................. Poster 068 Cross, Timothy A. ........................ Poster 329 Crouch, Ron ................................. Poster 227 Crull, George B. ........................... Poster 281 Crull, George B. ........................... Poster 282 da Silva Nunes, Luiza Maria ........ Poster 120 da Silva Nunes, Luiza Maria ........ Poster 116 Dalal, Naresh ............................... Poster 353 Darpolor, Moses .................. WOE 5:35-5:50 Das, Bibhuti ...................... FOB 11:35-11:50

Das, Ranabir ................................ Poster 190 Davis, Michael .............................. Poster 364 Davis, Ryan .................................. Poster 166 Davis-Harrison, Rebecca ............. Poster 009 Davis-Harrison, Rebecca ............. Poster 330 Daviso, Eugenio ................ FOB 11:50-12:05 Daviso, Eugenio ........................... Poster 144 Daviso, Eugenio ........................... Poster 188 Daviso, Eugenio ........................... Poster 266 Dawe, Louise ............................... Poster 338 Day, Graeme ................................ Poster 377 Dayie, Kwaku ............................... Poster 070 Dayie, T. Kwaku ........................... Poster 011 de Paepe, Gael ............................ Poster 367 de Queiroz Monteiro, Robson ...... Poster 050 De Vera, Ian Mitchelle .................. Poster 048 Debelouchina, Galia..................... Poster 325 DeBruhl, Nanette ......................... Poster 164 Deelchand, Dinesh....................... Poster 119 DeKoster, Gregory ....................... Poster 104 del Río-Portilla, Federico ............. Poster 067 Demco, Dan E. ............................. Poster 110 Demetrio, Elena ........................... Poster 081 Demirci, Fatih ............................... Poster 276 Dempah, Elodie ........................... Poster 387 Deng, Hexiang ............................. Poster 240 Denning, Mark .................. WOC 12:05-12:20 Dente, Axel D. .............................. Poster 113 DeRocher, Ronald ............ FOB 11:50-12:05 DeRocher, Ronald ....................... Poster 188 DeRose, Eugene F ...................... Poster 010 Deschamps, Michael .................... Poster 347 Devience, Stephen ........... WOC 11:35-11:50 Dey, Krishna ................................ Poster 364 Dick-Perez, Marilu ........................ Poster 322 Diehl, Annete ............................... Poster 030 Diehl, Carl ............................. TOD 5:35-5:50 Ding, Shangwu ............................. Poster 358 Ding, Shangwu ............................. Poster 356 Dixon, Nicholas E. ........................ Poster 315 Do, Van ........................................ Poster 176 Dobson, Chris .............................. Poster 325 Dodd, Stephen ............................. Poster 183 Dodevski, Igor .............................. Poster 201 Doetsch, Volker ............................ Poster 197 Dominguez, Santi......................... Poster 302 Donahue, Patrick ......................... Poster 054 Dorai, Kavita ................................ Poster 089 Doss, George ............................... Poster 292 Dovell, Sanaz ............................... Poster 062 Drover, Marcus ............................ Poster 338 Dudenko, Dmitri ........................... Poster 386 Dudenko, Dmytro ......................... Poster 079 Duff, Karen ................................... Poster 170 Dugar, Sneha ............................... Poster 353 Dumez, Jean-Nicolas ................... Poster 377 Dunkerley, David .......................... Poster 178 Dunn, Ben .................................... Poster 048 Duraiswami, Ramani .................... Poster 070 Dutta, Supratik ............................. Poster 047 Dvoyashkin, Muslim ..................... Poster 130 Dvoyashkin, Muslim ..................... Poster 109 Eddy, Matthew T. ................. MOD 4:50-5:05 Eddy, Matthew T. .............. MOB 12:05-12:20 Edelhoff, Daniel .................... WOE 5:20-5:35 Edison, Arthur .............................. Poster 215 Edison, Arthur ....................... MOE 5:05-5:20 Edison, Arthur .............................. Poster 179 Edmonds, Katherine A. ................ Poster 025 Eigenbrodt, Edwin ........................ Poster 178 Eliav, Uzi ............................. ThOA 9:20-9:35

INDEX OF AUTHORS


Page 113

Ellis, Heidi J.C. ............................. Poster 301 Ellis, Paul ..................................... Poster 184 Elyashberg, Mikhail ...................... Poster 300 Emami, Kiarash ........................... Poster 152 Emami, Kiarash ................... WOE 5:35-5:50 Emsley, Lyndon ........................... Poster 315 Emsley, Lyndon ........................... Poster 377 Emsley, Lyndon ........................... Poster 374 Emsley, Lyndon ................ MOB 11:50-12:05 Emsley, Lyndon ........................... Poster 148 Emsley, Lyndon .............. ThOC 11:35-11:50 Emwas, Abdul-Hamid .................. Poster 096 Endo, Yuki ................................... Poster 181 Endo, Yuki ...........................TOA 9:50-10:05 Engelke, Frank ............................. Poster 268 Entzminger, George ..................... Poster 184 Ernst, Benedikt .................... WOE 5:20-5:35 Ernst Scholtz Smith, Pieter ......................................... WOB 12:05-12:20 Espy, Michelle A. ......................... Poster 087 Espy, Michelle A. ......................... Poster 086 Fahim, Arjang .............................. Poster 082 Falco Cobra, Paulo ...................... Poster 120 Fang, Fang ......................ThOB 11:10-11:35 Fanucci, Gail ................................ Poster 032 Fanucci, Gail ................................ Poster 048 Farnan, Ian ....................... TOC 11:10-11:35 Farooq, Hashim ........................... Poster 247 Farooq, Hashim ............... WOC 11:50-12:05 Farooq, Hashim ........................... Poster 123 Farver, Suzanne .......................... Poster 307 Fawzi, Nicolas ................... MOB 11:35-11:50 Fejzo, Jasna ....................ThOB 11:35-11:50 Felletti, Michele ............... ThOC 11:35-11:50 Felletti, Michele ............................ Poster 315 Felli, Isabella C. ................ MOB 11:50-12:05 Felmy, Andrew R. ........................ Poster 344 Feng, Ju ............................ TOC 12:05-12:20 Feng, Ju ....................................... Poster 242 Feng, Ju ....................................... Poster 344 Feng, Yesu .................................. Poster 126 Fenwick, Matthew ........................ Poster 301 Fey, Michael ................................ Poster 123 Fey, Michael .................... WOC 11:50-12:05 Fey, Michael E. ............................ Poster 177 Fiala, Radovan ............................. Poster 003 Field, Timothy R. .......................... Poster 118 Figueroa-Villar, Jose Daniel ......... Poster 291 Fijalek, Zbigniew .......................... Poster 217 Fischer, Christian ......................... Poster 274 Fitzpatrick, Anthony ..................... Poster 325 Foguel, Debora ............................ Poster 030 Fontana, Francesca .........ThOB 11:50-12:05 Ford, Joseph ..................... TOC 12:05-12:20 Fox, Daniel ................................... Poster 034 Franco, Aldo ................................ Poster 062 Franks, Trent .................. ThOC 11:35-11:50 Franzoni, María Belén ......... WOA 8:30-8:55 Frederick, Thomas ....................... Poster 049 Fredriksson, Jonas ...................... Poster 041 Freedberg, Daron ........................ Poster 288 Freedberg, Daron ............ WOB 11:50-12:05 Freeman, Matthew ....................... Poster 117 Freiburger, Lee ............................ Poster 108 Freites, Alfredo ............................ Poster 004 Froehlke, Michael ........................ Poster 114 Fry, Elizabeth A. .......................... Poster 189 Fry, Roderick ............................... Poster 382 Frydman, Lucio ............................ Poster 228 Frydman, Lucio ..................... MOD 5:35-5:50 Frydman, Lucio ................ WOB 12:05-12:20

Frydman, Lucio ................... TOB 12:25-1:00 Fu, Riqiang .................................. Poster 353 Fu, Riqiang ....................... TOC 11:35-11:50 Fu, Riqiang .................................. Poster 329 Fu, Yinan ............................. WOD 4:50-5:05 Fujiwara, Toshimichi .......... WOA 9:50-10:05 Furet, Eric .................................... Poster 347 Furihata, Kazuo ........................... Poster 209 Furihata, Kazuo ........................... Poster 254 Furtig, Boris ......................... WOD 4:00-4:25 Furuyama, Jon K. ........................ Poster 164 Fushman, David ........................... Poster 070 Gajan, David ................................ Poster 148 Galiana, Gigi ................................ Poster 258 Galinsky, Yoram .......................... Poster 186 Gan, Zhehong .............................. Poster 040 Gan, Zhehong .............................. Poster 369 Gan, Zhehong .............................. Poster 381 Ganguly, Manjori .......................... Poster 054 Ganssle, Paul ....................... FOA 9:35-9:50 Garbacz, Piotr .............................. Poster 097 Garbacz, Piotr .............................. Poster 273 Garcia, Angel ............................... Poster 279 Garcia Manteiga, Jose .... ThOB 11:50-12:05 Gardeniers, Han .......................... Poster 159 Garvey, Mark ............................... Poster 274 Garwood, Michael ........................ Poster 101 Garwood, Michael ........................ Poster 119 Garwood, Michael ................. TOE 5:20-5:35 Gath, Julia .................................... Poster 316 Gaude, Edoardo ............. ThOB 11:50-12:05 Gayathri, Chakicherla .................. Poster 212 Geissler, Brett .............................. Poster 008 Gennis, Robert ...................... TOA 9:20-9:35 George, John ............................... Poster 086 George, Julia ............................... Poster 328 Geppi, Marco ................... WOC 12:05-12:20 Gerald, Rex .................................. Poster 225 Gerald, Rex .................................. Poster 372 Ghatak, Somenath ....................... Poster 277 Ghatak, Somenath ....................... Poster 287 Ghiviriga, Ion ................................ Poster 303 Ghosh, Rajat ................................ Poster 155 Ghosh, Rajat ................................ Poster 154 Ghosh, Rajat ................................ Poster 137 Giacomini, Eric ............................. Poster 186 Gibbs, David ................................ Poster 246 Gil, Roberto R. ............................. Poster 212 Gilad, Assaf .......................... TOE 5:05-5:20 Giller, Karin ......................... ThOD 4:50-5:05 Gimi, Barjor .................................. Poster 271 Gimi, Barjor .................................. Poster 085 Giraudeau, Patrick ............... WOE 4:50-5:05 Giraudeau, Patrick ....................... Poster 206 Girgis, Mark .......................... TOE 5:35-5:50 Glass, Karen ................................ Poster 058 Glockshuber, Rudi ....................... Poster 335 Go, Vay ................................. TOE 5:35-5:50 Gold, Barry ................................... Poster 054 Goldfarb, David ................... ThOD 4:25-4:50 Golotvin, Sergey .......................... Poster 286 Gomes, José R. B. ....................... Poster 388 Gomez, Agustín ........................... Poster 380 Gomez, John ............................... Poster 086 Gómez-Reyes, José Félix ... ThOE 5:35-5:50 Gonnelli, Leonardo ........... MOB 11:50-12:05 Good, Jeremy .............................. Poster 261 Goodson, Boyd M. ....................... Poster 147 Goodson, Boyd M. ....................... Poster 162 Goodson, Boyd M. ....................... Poster 160 Gor’kov, Peter L. .......................... Poster 185

Gor'kov, Peter .............................. Poster 040 Gor'kov, Peter L. .......................... Poster 177 Gor'kov, Peter L. ............... TOC 11:35-11:50 Gossert, Alvar ..................... ThOD 4:50-5:05 Goswami, Mithun ......................... Poster 359 Gottardo, Federico ....................... Poster 029 Gowda, Nagana ........................... Poster 251 Gozani, Or .................................... Poster 058 Goze-Bac, Christophe........... MOE 4:50-5:05 Graf, Robert ................................. Poster 079 Grandinetti, Philip J. ..................... Poster 272 Grandinetti, Philip J. ..................... Poster 364 Grandinetti, Philip J. ..................... Poster 343 Grant, Christopher V. ................... Poster 115 Grant, Christopher V. ................... Poster 175 Grant, Samuel .............................. Poster 271 Gravel, Andrée ............................. Poster 005 Gray, George ............................... Poster 326 Grey, Clare P. ..................... ThOA 9:35-9:50 Grey, Clare P. .............................. Poster 374 Griesinger, Christian ........ WOB 11:35-11:50 Griesinger, Christian ........... ThOD 4:50-5:05 Griffin, Robert ............................... Poster 325 Griffin, Robert ............................... Poster 266 Griffin, Robert ............................... Poster 188 Griffin, Robert .................... MOB 12:05-12:20 Griffin, Robert ............................... Poster 150 Griffin, Robert ............................... Poster 127 Griffin, Robert ............................... Poster 144 Griffin, Robert ............................... Poster 180 Griffin, Robert ....................... MOD 4:50-5:05 Griffin, Robert G. ............... FOB 11:50-12:05 Griffin, Robert G. .......................... Poster 141 Gronenborn, Angela..................... Poster 045 Gronenborn, Angela..................... Poster 040 Groome, Kirsten ........................... Poster 160 Grosso, John ................................ Poster 281 Grunin, Leonid ............................. Poster 361 Gruppi, Francesca ................ MOE 5:20-5:35 Gruschus, James ......................... Poster 044 Gryk, Michael R. .......................... Poster 301 Guedes de Andrade, Flavia ......... Poster 030 Guentert, Peter ............................ Poster 335 Guirlando, Rodolfo ............ MOB 11:35-11:50 Guittet, Eric .................................. Poster 311 Gumerov, Nail A. .......................... Poster 070 Güntert, Peter .............................. Poster 197 Güntert, Peter .............................. Poster 072 Guo, Qianni .................................. Poster 143 Gupta, Ashish .............................. Poster 249 Gust, brogan ................................ Poster 147 Gustavsson, Martin ........... FOB 12:05-12:30 Habenstein, Birgit ......................... Poster 316 Hagaman, Edward W. .................. Poster 103 Håkansson, Pär ........................... Poster 154 Hakkarainen, Hanne ............. TOE 5:20-5:35 Halidi, El Mohamed ............... MOE 4:50-5:05 Hall, Kathleen ............................... Poster 104 Halse, Meghan ............................. Poster 377 Han, Fei ....................................... Poster 259 Han, Kee Sung ............................. Poster 103 Han, Oc Hee ................................ Poster 345 Han, Sohyun ................................ Poster 090 Han, Songi ................................... Poster 142 Han, Yun ...................................... Poster 045 Han, Yun ...................................... Poster 040 Hanes, Justin ........................ TOE 5:05-5:20 Hansen, D. Flemming .................. Poster 074 Hansen, Michael Ryan ................. Poster 079 Harbison, Gerard ......................... Poster 385 Hardy, Micaël ............................... Poster 232

INDEX OF AUTHORS


Page 114

Harris, Kristopher J. .............. MOD 5:35-5:50 Harris, Kristopher J. ..................... Poster 349 Hashami, Zohreh ......................... Poster 128 Hata, Yoshiaki .............................. Poster 239 Haupt, Erhard T.K. ....................... Poster 125 Hayamizu, Kikuko ........................ Poster 094 Hayes, Sophia E. ......................... Poster 340 Hayes, Sophia E. .................. MOE 4:00-4:25 Haze, Olesya ............................... Poster 127 Haze, Olesya ............................... Poster 150 He, Ping ....................................... Poster 160 He, Qiuhong ................................. Poster 168 Hebbar, Sankeerth ....................... Poster 211 Heinrich, John .............................. Poster 387 Heng, Xiao .............................TOA 8:30-8:55 Hengge, Alvan ............................. Poster 028 Hennig, Jürgen ......................TOE 4:00-4:25 Hennig, Mirko ............................... Poster 051 Henning, Stefan ................... WOE 5:20-5:35 Hermida, Oscar ................. MOB 12:05-12:20 Hernández, Gonzalo ............ThOE 4:50-5:05 Hernández-Vázquez, Liliana........ Poster 208 Herrera, Alvaro I .......................... Poster 237 Herrmann, Torsten ............ MOB 11:50-12:05 Herrmann, Torsten ....................... Poster 315 Herzfeld, Judith ............................ Poster 266 Herzfeld, Judith ............................ Poster 144 Herzfeld, Judith ............................ Poster 180 Herzfeld, Judith ............................ Poster 188 Herzfeld, Judith ..................FOB 11:50-12:05 Hilcenko, Christine .................TOA 8:55-9:20 Hilser, Vincent ...................... WOD 4:50-5:05 Hiltunen, Yrjo ............................... Poster 361 Hilty, Christian .............................. Poster 131 Hilty, Christian .................. WOB 11:35-11:50 Hilty, Christian .............................. Poster 129 Hlova, Ihor Z. ............................... Poster 354 Ho, Chien ..................................... Poster 064 Hoatson, Gina .............................. Poster 100 Hoch, Jeffrey C. .................TOB 10:45-11:20 Hoch, Jeffrey C. ........................... Poster 363 Holland, Daniel ......................TOA 9:35-9:50 Holland, Gregory P. ..................... Poster 036 Holland, Gregory P. ..................... Poster 167 Holroyd, Chloe M. ........................ Poster 202 Hong, Mei .................................... Poster 322 Hong, Mei .................................... Poster 319 Hong, Mei .................................... Poster 320 Hong, Mei .................................... Poster 308 Hong, Mei ............................. MOD 4:25-4:50 Hooker, Jerris .............................. Poster 215 Hooker, Jerris ....................... MOE 5:05-5:20 Hooker, Jerris .............................. Poster 179 Hoop, Cody .................................. Poster 336 Hoop, Cody L. .............................. Poster 323 Hori, Shunsuke ............................ Poster 339 Hornak, Joseph ............................ Poster 102 Hoshi, Minako .............................. Poster 317 Hou, Guangjin .............................. Poster 006 Hou, Guangjin .............................. Poster 363 Hou, Guangjin .............................. Poster 045 Hou, Guangjin .............................. Poster 040 Hou, Jianbo ....................... TOC 11:50-12:05 Hou, Jianbo .................................. Poster 236 Hovav, Yonatan ........................... Poster 136 Howe, Peter ................................. Poster 296 Hoyt, David W. .................... ThOD 5:35-5:50 Hoyt, David W. .................. TOC 12:05-12:20 Hoyt, David W. ............................. Poster 114 Hsu, Chaohsiung ...................TOE 5:35-5:50 Hu, Bingwen ................................ Poster 367

Hu, Fangyu .................................. Poster 254 Hu, Jian Zhi ....................... TOC 12:05-12:20 Hu, Jian Zhi .................................. Poster 344 Hu, Jian Zhi ......................... ThOD 5:35-5:50 Hu, Jian Zhi .................................. Poster 114 Hu, Kan-Nian .................. ThOC 11:10-11:35 Hu, Mary ...................................... Poster 344 Hu, Mary ........................... TOC 12:05-12:20 Huang, Danting ............................ Poster 389 Huang, Hongzhou ........................ Poster 237 Huang, Rui-Yi .............................. Poster 356 Huang, Xi ..................................... Poster 032 Huber, Alexandra ......................... Poster 348 Huber, Matthias ........................... Poster 335 Hugon, Cedric ..................... FOA 9:50-10:05 Hui, Hongxiang ..................... TOE 5:35-5:50 Hume, Alan ...................... WOC 11:50-12:05 Hume, Alan .................................. Poster 123 Humpfer, Eberhard ......... ThOB 11:10-11:35 Hung, Ivan ................................... Poster 369 Hung, Ivan ................................... Poster 040 Hung, Ivan ................................... Poster 381 Hung, Ivan ................................... Poster 068 Hung, Ivan ................................... Poster 177 Hung, Tiffany ............................... Poster 058 Hurlimann, Martin D. .................... Poster 176 Hussain, Muhammad ................... Poster 096 Hutchins, Howard ............ WOC 11:50-12:05 Hutchins, Howard ........................ Poster 123 Hwang, Ryeo Yun ........................ Poster 345 Hwang, Tsang-Lin ........................ Poster 252 Hyberts, Sven G. ................. WOA 9:35-9:50 Idehara, Toshitaka ............. WOA 9:50-10:05 Idiyatullin, Djaudat ................ TOE 5:20-5:35 Iglesius, Isaac .............................. Poster 305 Igumenova, Tatyana .................... Poster 257 Igumenova, Tatyana I. ................. Poster 022 Ikäläinen, Suvi ............................. Poster 138 Ikeda, Ryosuke .................. WOA 9:50-10:05 Ikpo, Nduka .................................. Poster 338 Ilioaia, Oana ................................. Poster 311 Ingo, Carson ........................ WOE 5:05-5:20 Inoue, Masafumi .......................... Poster 317 Irausquin, Stephanie ............. TOD 4:50-5:05 Irausquin, Stephanie .................... Poster 076 Isern, Nancy ................................. Poster 114 Ishii, Masaru ................................ Poster 152 Ishii, Yoshitaka ............................. Poster 317 Ishii, Yoshitaka .................... TOA 9:50-10:05 Ishii, Yoshitaka ............................. Poster 313 Ishii, Yoshitaka ............................. Poster 078 Ishima, Rieko ............................... Poster 111 Ishima, Rieko ............................... Poster 027 Ishima, Rieko ............................... Poster 017 Ishimaru, Daniella ........................ Poster 051 Jackowski, Karol .......................... Poster 273 Jacob, Jaison .................. ThOB 11:35-11:50 Jaeger, Christian .......................... Poster 348 Janco, Miroslav ............................ Poster 234 Jannin, Sami ........................ WOA 8:55-9:20 Jaremko, Lukasz .......................... Poster 107 Jaremko, Mariusz ........................ Poster 106 Jaroniec, Christopher ................... Poster 325 Jaszunski, Michal ......................... Poster 273 Jawla, Sudheer ............................ Poster 180 Jawla, Sudheer ............................ Poster 188 Jawla, Sudheer K. ............. FOB 11:50-12:05 Jayasundar, Rama ....................... Poster 293 Jayasundar, Rama ....................... Poster 277 Jean-Francois, Frantz L. .............. Poster 012 Jehle, Stefan ................................ Poster 315

Jehle, Stefan ................... ThOC 11:35-11:50 Jelescu, Ileana ...................... TOE 4:50-5:05 Jensen, Malene R. .......... ThOC 11:35-11:50 Jerschow, Alexej .......................... Poster 270 Jerschow, Alexej ................... MOE 5:20-5:35 Jerschow, Alexej ............... ThOA 9:50-10:05 Jerschow, Alexej ................. ThOA 9:35-9:50 Jerschow, Alexej .......................... Poster 259 Ji, Fangling ................................... Poster 265 Jiang, Bin ..................................... Poster 283 Jindal, Ashish ............................... Poster 157 Joe, Murphy-Boesch .................... Poster 183 Johannessen, Ole G. ....... WOC 12:05-12:20 Johnston, Karen ........................... Poster 350 Jones, Louis ................................. Poster 370 Jung, Jinwon ................................ Poster 045 Jung, Kwang-Hwang .................... Poster 334 Kaderavek, Pavel ......................... Poster 003 Kaderavek, Pavel .................. TOD 5:35-5:50 Kadlecek, Stephen ....................... Poster 152 Kadlecek, Stephen J. ................... Poster 153 Kadlecek, Stephen J. ................... Poster 156 Kadlecek, Stephen J. ................... Poster 155 Kadlecek, Stephen J. ................... Poster 154 Kadlecek, Stephen J. ........... WOE 5:35-5:50 Kaerner, Andreas ............. WOB 11:10-11:35 Kainosho, Masatsune ......... TOA 9:50-10:05 Kang, Alvin ................................... Poster 056 Kaplan, Mohammed .............. FOA 8:55-9:20 Kar, Karunakar ............................. Poster 323 Kara, Huseyin .............................. Poster 153 Kara, Huseyin .............................. Poster 155 Kara, Huseyin .............................. Poster 154 Kara, Huseyin .............................. Poster 156 Karageorgos, Ioannis ................... Poster 023 Kaseman, Derrick ........................ Poster 272 Kaseman, Derrick ........................ Poster 369 Kaseman, Derrick C. .................... Poster 343 Kasinath, Vignesh ................ WOD 4:50-5:05 Katihar, Aakanksha ...................... Poster 109 Kautz, Roger ................................ Poster 275 Kawamura, Izuru .......................... Poster 334 Ke, Wealen .................................. Poster 358 Keeler, Eric .................................. Poster 272 Keeler, Eric G. .............................. Poster 343 Keenan, Caroline D...................... Poster 146 Kempf, Jim .......................... ThOD 4:25-4:50 Kennedy, Daniel ........................... Poster 124 Kennedy, Michael A. .................... Poster 248 Kentgens, Arno ............................ Poster 359 Kentgens, Arno ............................ Poster 159 Kern, Dorothee .................. MOB 10:45-11:10 Kerton, Francesca ........................ Poster 338 Keshari, Kayvan ........................... Poster 134 Keshari, Kayvan ........................... Poster 139 Khaneja, Navin ............................. Poster 362 Khaneja, Navin ............................. Poster 196 Khanna, Arjun .............................. Poster 117 Khetrapal, Cl ................................ Poster 249 Khirich, Gennady ......................... Poster 014 Khitrin, Anatoly .................. ThOA 9:50-10:05 Khorasanizadeh, Sepideh ............ Poster 060 Kidd, Bryce E. ................... TOC 11:50-12:05 Kiesewetter, Matthew................... Poster 127 Kijac, Aleksandra ......................... Poster 018 Kim, Jae ....................................... Poster 328 Kim, Jieun .................................... Poster 170 Kim, Jihan .................................... Poster 240 Kim, Seho .................................... Poster 031 Kinde, Monica .............................. Poster 385 Kingsley, Carolyn ......................... Poster 004

INDEX OF AUTHORS


Page 115

Kirby, Thomas .............................. Poster 010 Kiruluta, Andrew .......................... Poster 119 Kitamura, Masashi ....................... Poster 239 Kitamura, Masashi ....................... Poster 339 Kitchen, Jason .................. TOC 11:35-11:50 Kitchen, Jason A. ......................... Poster 177 Kitching, John ........................FOA 9:35-9:50 Knappe, Svenja .....................FOA 9:35-9:50 Knight, Michael J. ............. MOB 11:50-12:05 Kobayashi, Takeshi ..................... Poster 354 Koda, Masanori ............................ Poster 254 Kodali, Ravi .................................. Poster 336 Kodali, Ravindra .......................... Poster 323 Koers, Eline .........................FOA 8:55-09:20 Komlosh, Michal ................ThOA 9:20-09:35 Kong, Fangming .......................... Poster 297 Kong, Xueqian ............................. Poster 240 Koretsky, Alan .............................. Poster 183 Korhonen, Samuli-Petrus ............. Poster 075 Korzhnev, Dmitry ......................... Poster 065 Korzhnev, Dmitry ......................... Poster 061 Kosuga, Kosuke ................. WOA 9:50-10:05 Kovacs, Helena ................... ThOD 4:50-5:05 Kovacs, Zoltan ............................. Poster 157 Kovacs, Zoltan ............................. Poster 128 Kovacs, Zoltan ............................. Poster 135 Kozerski, Lech ............................. Poster 020 Kozerski, Lech ............................. Poster 217 Kozerski, Lech ............................. Poster 019 Kracke, Holger .....................FOA 8:30-08:55 Krasny, Libor ......................... TOD 5:35-5:50 Krishnamurthy, Sridevi ................. Poster 123 Krishnamurthy, Sridevi ..... WOC 11:50-12:05 Krishnan Achary, Damodaran ...... Poster 099 Krivdin, Leonid ............................. Poster 213 Kubicek, Karel .................. WOB 11:35-11:50 Kumar, Dinesh ............................. Poster 249 Kumar, Rajeev ................. WOC 11:50-12:05 Kumar, Rajeev ............................. Poster 123 Kumar, Uttam ............................... Poster 249 Kumari, Divya .............................. Poster 211 Kunze, Micha B. A. ...................... Poster 074 Kupce, Eriks ................................. Poster 306 Kurek, Piotr .................................. Poster 159 Kurhanewicz, John ...................... Poster 134 Kurhanewicz, John ...................... Poster 139 Kurita, Junichi .............................. Poster 306 Kurizki, Gershon .............. WOB 12:05-12:20 Kurotsu, Takuzo ........................... Poster 339 Kurotsu, Takuzo ........................... Poster 239 Kurzynoga, Dariusz ..................... Poster 019 Kutateladze, Tatiana .................... Poster 058 Kuzma, Nicholas .......................... Poster 156 Kuzma, Nicholas N. ............. WOE 5:35-5:50 Kuzma, Nicholas N. ..................... Poster 155 Kuzma, Nicholas N. ..................... Poster 154 Kuzma, Nicholas N. ..................... Poster 153 Kuznetsova, Anna ........................ Poster 037 Kwak, Ja Hun .................... TOC 12:05-12:20 Kwok, Wingchi Edmund ............... Poster 102 Ladizhansky, Vladimir .................. Poster 325 Ladizhansky, Vladimir .................. Poster 332 Ladizhansky, Vladimir .................. Poster 334 Lafon, Olivier ................................ Poster 132 Lafon, Olivier ................................ Poster 379 Lafon, Olivier ................................ Poster 268 Lafon, Olivier ......................... MOD 5:05-5:20 Lafon, Olivier ................................ Poster 371 Lafon, Olivier ................................ Poster 367 Lai, Angel ..................................... Poster 314 Lam, Yun Wah ............................. Poster 250

Lange, Adam ...................... ThOD 5:05-5:20 Lange, Sascha ................ ThOC 11:35-11:50 Langeslay, Derek ......................... Poster 001 Laplante, Steven .......................... Poster 290 Larda, Sacha ............................... Poster 046 Laustsen, Christoffer ............ WOA 9:20-9:30 Le Bihan, Denis .................... TOE 4:50-5:05 Le Bihan, Denis ........................... Poster 186 Le Pollès, Laurent ........................ Poster 347 Leblanc, Regan ............................ Poster 013 Led, Jens J .................................. Poster 074 Lee, Donghan .................. WOB 11:35-11:50 Lee, Donghan ..................... ThOD 4:50-5:05 Lee, Jae-Seung ........................... Poster 270 Lee, Jae-Seung ........................... Poster 259 Lee, Jae-Seung ................ ThOA 9:50-10:05 Lee, Jennifer C. ........................... Poster 044 Lee, Jung Ho ............................... Poster 151 Lee, Phil ....................................... Poster 170 Lee, Phil ....................................... Poster 169 Lee, Sang Man ............................ Poster 345 Lee, Shin ...................................... Poster 328 Lee, Youngbok ................. WOB 11:35-11:50 Lee, Youngbok ............................. Poster 131 Lehtivarjo, Juuso .......................... Poster 075 Leick, Sabine ....................... WOE 5:20-5:35 Lelli, Moreno ................................ Poster 148 Lemkau, Luisel ............................. Poster 328 Leonard, Sarah ............................ Poster 384 Lesage, Anne ............................... Poster 315 Lesage, Anne ........................ MOE 4:25-4:50 Lesage, Anne ............................... Poster 148 Lesage, Anne .................. ThOC 11:35-11:50 Levitt, Malcolm ..................... WOA 9:20-9:30 Levitt, Malcolm ............................. Poster 154 Levitt, Malcolm ................. WOC 12:05-12:20 Levstein, Patricia R. ..................... Poster 380 Levstein, Patricia R. ..................... Poster 113 Levstein, Patricia Rebeca ... ThOE 4:00-4:25 Lewis, David ................................ Poster 387 Lewis, Kenneth ............................ Poster 248 Li, Conggang ............................... Poster 381 Li, Haidong ................................... Poster 143 Li, Hongde ................................... Poster 250 Li, Wenjing ................................... Poster 352 Li, Yang ........................................ Poster 262 Li, Zhao ................................. TOE 5:35-5:50 Li, Zhao ........................................ Poster 143 Liao, Shu Yu ................................ Poster 319 Liimatainen, Timo ........................ Poster 101 Liimatainen, Timo ................. TOE 5:20-5:35 Lilly Thankamony, Aany Sofia ..... Poster 132 Lima, Luize .................................. Poster 050 Lin, Ping-Chang ........................... Poster 169 Lin, Yung-Ya ......................... TOE 5:35-5:50 Linden, Arne ................... ThOC 11:35-11:50 Lindorff-Larsen, Kresten ..... TOD 4:25-04:50 Lingel, Andreas ............... ThOB 11:35-11:50 Lingwood, Mark D. ............ TOC 11:50-12:05 Linser, Rasmus J. ........................ Poster 199 Lipton, Andrew ............................. Poster 040 Lipton, Andrew S. ........................ Poster 114 Liu, Chaoyang .............................. Poster 077 Liu, Guanshu ........................ TOE 5:05-5:20 Liu, Hui ......................................... Poster 260 Liu, Jun ............................. TOC 12:05-12:20 Liu, Maili ....................................... Poster 283 Liu, Mali ....................................... Poster 381 Liu, Ting ....................................... Poster 355 Liu, Xiaoli ..................................... Poster 381 Llovera, Ligia ...................... ThOE 5:05-5:20

Lockhart, Alexander ..................... Poster 071 Löhr, Frank ................................... Poster 197 London, Robert ............................ Poster 071 London, Robert ............................ Poster 010 Long, Jeffrey ................................ Poster 240 Long, Joanna ............................... Poster 037 Long, Joanna R. ........................... Poster 307 Longo, Liam ................................. Poster 331 Longstaffe, James............ WOC 11:50-12:05 Longstaffe, James........................ Poster 231 Longstaffe, James G. ................... Poster 360 Lopes, João H. ............................. Poster 333 Lopez, Christopher....................... Poster 093 Loquet, Antoine ............................ Poster 319 Loquet, Antoine ................... ThOD 5:05-5:20 Loria, J. Patrick ............................ Poster 028 Loria, J. Patrick ............................ Poster 014 Lorieau, Justin ................... MOB 11:10-11:35 Loring, John ........................ ThOD 5:35-5:50 Louis, John ........................ MOB 11:10-11:35 Lu, George J. ............................... Poster 318 Lu, Junxia ........................ ThOC 11:10-11:35 Lu, Xingyu .................................... Poster 132 LU, Xingyu ........................... MOD 5:05-5:20 Lubach, Joseph ............................ Poster 387 Luca, Sorin ................................... Poster 016 Luchinat, Claudio ......................... Poster 127 Luchsinger, Sarah ........................ Poster 274 Lucier, Bryan E. G........................ Poster 349 Lucier, Bryan E.G................. MOD 5:35-5:50 Ludlow, Douglas .......................... Poster 225 Lumata, Lloyd .............................. Poster 157 Lumata, Lloyd .............................. Poster 128 Lumata, Lloyd .............................. Poster 135 Luna, Hector ................................ Poster 208 Luo, Qing ..................................... Poster 143 Luo, Zhiping ................................. Poster 237 Lupulescu, Adonis................ MOD 5:35-5:50 Lyons, Leslie J. ............................ Poster 238 Maas, Werner .............................. Poster 325 Maas, Werner E. .......................... Poster 123 Maas, Werner E. .............. WOC 11:50-12:05 Maas, Werner E. .......................... Poster 148 Macdonald, Peter ......................... Poster 314 Machado, Luciana Elena .... ThOE 5:20-5:35 MacPhee, Cait ............................. Poster 325 Madsen, Louis A ............... TOC 11:50-12:05 Madsen, Louis A .......................... Poster 236 Mafra, Luis ................................... Poster 388 Mafra, Luis ................................... Poster 079 Mafra, Luís ................................... Poster 386 Magalhães, Alviclér ...................... Poster 333 Magalhães, Alviclér ...................... Poster 243 Magin, Richard ............................. Poster 271 Magnelind, Per ............................. Poster 087 Magnelind, Per ............................. Poster 086 Mahieu-Willame, Laurent ...... MOE 4:50-5:05 Majors, Paul ................................. Poster 114 Mak-Jurkauskas, Melody L. ......... Poster 141 Makriyannis, Alexandros .............. Poster 023 Makulski, Wlodzimierz ................. Poster 273 Malloy, Craig ................................ Poster 157 Malloy, Craig R. ........................... Poster 135 Maltsev, Sergey ........................... Poster 337 Maly, Thorsten ............................. Poster 171 Mamone, Salvatore .......... WOC 12:05-12:20 Mamyan, Suren ............................ Poster 224 Manasseh, Philip .......................... Poster 154 Manasseh, Philip .......................... Poster 155 Mandal, Soumyajit ....................... Poster 173 Mandal, Soumyajit ....................... Poster 172

INDEX OF AUTHORS


Page 116

Mandal, Soumyajit ....................... Poster 176 Mandal, Soumyajit ....................... Poster 187 Manetsch, Roman ........................ Poster 285 Mangia, Silvia .............................. Poster 101 Mangia, Silvia ........................TOE 5:20-5:35 Mao, Wenping .............................. Poster 177 Mao, Wenping .............................. Poster 185 Marchetti, Alessandro .................. Poster 315 Marcotte, Isabelle ........................ Poster 005 Marcotte, Isabelle ........................ Poster 002 Marek, Antonin ............................. Poster 378 Margolis, Daniel ........................... Poster 164 Mari, Frank ................................... Poster 062 Mari, Silvia .......................ThOB 11:50-12:05 Markhasin, Evgeny ...................... Poster 188 Markhasin, Evgeny ...................... Poster 144 Markhasin, Evgeny ............FOB 11:50-12:05 Markley, John L. .......................... Poster 059 Markley, John L. .......................... Poster 033 Markley, John L. .......................... Poster 074 Markus, Michelle .......................... Poster 274 Marquardsen, Thorsten ....... WOD 4:00-4:25 Martin, Rachel W. ........................ Poster 004 Martineau, Charlotte .................... Poster 268 Martineau, Charlotte .................... Poster 379 Maruenda, Helena ....................... Poster 212 Mason, Claire ............................... Poster 315 Masoom, Hussain ............ WOC 11:50-12:05 Masoom, Hussain ........................ Poster 123 Massiot, Dominique ..................... Poster 347 Masterson, Larry .......................... Poster 066 Matei, Helena ............................... Poster 062 Matlashov, Andrei ........................ Poster 086 Matlashov, Andrei ........................ Poster 087 Matson, Gerald ............................ Poster 260 Matsuki, Yoh ...................... WOA 9:50-10:05 May, Jody .................................... Poster 095 Mazali, Italo O. ............................. Poster 333 Mazur, Adam ................... WOB 11:35-11:50 Mcdermott, Ann .............. ThOC 10:45-11:10 McElheny, Dan ............................ Poster 078 McGarvey, David ......................... Poster 382 McGarvey, David ......................... Poster 210 McLean, Janel ............................. Poster 095 McLean, John .............................. Poster 095 Mcmahon, Michael T. ............TOE 5:05-5:20 McNamara, Daniel ....................... Poster 282 McNees, C. Ruth ......................... Poster 095 Mehta, Hardeep ........................... Poster 114 Mehta, Hardeep ................ TOC 12:05-12:20 Meier, Beat .................................. Poster 335 Meier, Beat .................................. Poster 316 Meiler, Jens ..................... WOB 11:35-11:50 Melki, Ronald ............................... Poster 316 Melo, Homero J. F. ...................... Poster 243 Melquiond, Adrien ........... ThOC 11:50-12:05 Meneses Ramirez, Erick Alejandro ............................................. WOD 5:35-5:50 Merritt, Matthew E. ....................... Poster 157 Merritt, Matthew E. ....................... Poster 128 Merritt, Matthew E. ....................... Poster 149 Merritt, Matthew E. ....................... Poster 135 Miao, Yimin .................................. Poster 329 Michaeli, Shalom ......................... Poster 101 Michaeli, Shalom ...................TOE 5:20-5:35 Michaelis, Vladimir K. .................. Poster 188 Michaelis, Vladimir K. .................. Poster 141 Michaelis, Vladimir K. ........FOB 11:50-12:05 Michaelis, Vladimir K. .................. Poster 144 Michal, Carl A. ................. WOC 11:10-11:35 Middlemiss, Derek S. ................... Poster 374

Mikiewicz-Syguła, Diana .............. Poster 019 Milbradt, Alexander G. ......... WOA 9:35-9:50 Miletti, Teresa .............................. Poster 055 Miller, Karla ......................... ThOA 8:30-8:55 Milne, Jacqueline E. ..................... Poster 252 Miroux, Bruno .............................. Poster 311 Mishra, Rakesh ............................ Poster 323 Mitchell, Odingo ........................... Poster 375 Mittermaier, Anthony ............ WOD 5:35-5:50 Mittermaier, Anthony K. ............... Poster 108 Mittermaier, Anthony K. ............... Poster 055 Miyakawa, Takuya ....................... Poster 254 Mobley, T. Andrew ....................... Poster 238 Mohr, Daniel ................................ Poster 228 Mokwa, Wilfried ........................... Poster 174 Mollhagen, Ariel ........................... Poster 225 Monastyrskyi, Andrii ..................... Poster 285 Monecke, Peter ................ WOB 11:35-11:50 Monette, Martine .......................... Poster 123 Monette, Martine .............. WOC 11:50-12:05 Montag, Tobias ............................ Poster 206 Moon, Chulsoon ........................... Poster 088 Mooney, Victoria L. ...................... Poster 189 Moore, Jeremy ............................. Poster 340 Moorman, Veronica ............. WOD 4:50-5:05 Morales, Krystal A. ....................... Poster 022 Morgan, Steven ........................... Poster 121 Morgan, Steven ........................... Poster 376 Moroz, Greg ................................. Poster 147 Morris, Gareth .............................. Poster 204 Morris, Gareth A. ......................... Poster 202 Morris, Peter ................................ Poster 162 Morrissey, James ......................... Poster 330 Morrissey, James ......................... Poster 009 Mote, Kaustubh ............................ Poster 321 Mozes, Christina .......................... Poster 051 Mueller, Geoffrey A. ..................... Poster 071 Mueller, Karl ................................. Poster 114 Mueller, Karl ................................. Poster 346 Mueller, Leonard J. ...................... Poster 312 Mueller, Leonard J. .............. MOD 4:00-4:25 Mueller, Leonard J. ...................... Poster 080 Muennemann, Kerstin .......... WOA 8:30-8:55 Mulhall, Daniel ............................. Poster 049 Munson, Eric ................................ Poster 387 Müntjes, Jutta .............................. Poster 174 Muradyan, Iga .............................. Poster 147 Murata, Yasujiro ............... WOC 12:05-12:20 Murphy, Denette .......................... Poster 282 Murray, Dylan .............................. Poster 068 Musco, Giovanna ............ ThOB 11:50-12:05 Mustonen, J. Peter ....................... Poster 124 Myint, Wazo Z. ............................. Poster 017 Myint, Wazo Z. ............................. Poster 111 Nagarajan, Rajakumar ................. Poster 164 Nagarajarao, Suryaprakash ......... Poster 211 Nair, Sankar ................................. Poster 109 Nakamura, Shinji ............... WOA 9:50-10:05 Nakazawa, Chikako T. ................. Poster 339 Nand, Deepak ................. ThOC 11:50-12:05 Nanni, Emilio ................................ Poster 188 Nanni, Emilio ................................ Poster 180 Nanni, Emilio A. ................ FOB 11:50-12:05 Nargeot, Romuald ................. TOE 4:50-5:05 Nast, Robert ................................. Poster 179 Nast, Robert .......................... MOE 5:05-5:20 Nast, Robert ................................. Poster 215 Nath, Pulak .................................. Poster 178 Nativel, Eric ........................... MOE 4:50-5:05 Naumczuk, Beata ........................ Poster 020 Navarro-Ocaña, Arturo ................ Poster 208

Navarro-Vázquez, Armando ........ Poster 212 Navon, Gil ........................... ThOA 9:20-9:35 Nelson, Benjamin N. .................... Poster 387 Nemoto, Takahiro ........................ Poster 181 Nemoto, Takahiro ............... TOA 9:50-10:05 Nesbitt, Anna ........................ TOA 9:20-9:35 Nevzorov, Alexander A. ............... Poster 378 Newton, Hayley ............................ Poster 147 Newton, Hayley ............................ Poster 162 Ngo, Raymond ...................... TOE 5:35-5:50 Nguyen, Bao ................................ Poster 297 Ni, Qing ........................................ Poster 180 Nielsen, Anders B. ....................... Poster 362 Nielsen, Niels Chr. ....................... Poster 362 Nielsen, Niels Chr. ....................... Poster 365 Niemitz, Matthias ......................... Poster 075 Nietlispach, Daniel ................ TOA 9:35-9:50 Nieuwkoop, Andrew ..................... Poster 328 Nieuwkoop, Andrew ..................... Poster 326 Nieuwkoop, Andrew J. .......... TOA 9:20-9:35 Nikolaou, Peter ............................ Poster 147 Nikolskaya, Ekaterina .................. Poster 361 Nilsson, Mathias ........................... Poster 204 Nilsson, Mathias ........................... Poster 202 Nishiyama, Yusuke ...................... Poster 181 Nishiyama, Yusuke ............. TOA 9:50-10:05 Nordell, Bradley ........................... Poster 352 Norris, Scott E. ............................. Poster 288 Nozinovic, Senada ............... WOD 4:00-4:25 Nucci, Nathaniel ................... WOD 4:50-5:05 Nucci, Nathaniel ........................... Poster 201 Nuzzio, Kristin .............................. Poster 330 Oganesyan, Vadim ...................... Poster 121 Ogawa, Isamu .................... WOA 9:50-10:05 Ohkubo, Zenmei .......................... Poster 009 O'Keefe, Christopher ................... Poster 350 Oliveira-Silva, Rodrigo ........ ThOE 4:25-4:50 Ong, Ta-Chung ............................ Poster 141 Opella, Stanley J. ......................... Poster 175 Opella, Stanley J. ......................... Poster 318 Opella, Stanley J. .............. FOB 11:35-11:50 Opella, Stanley J. ......................... Poster 115 Oschkinat, Hartmut ...................... Poster 030 Oschkinat, Hartmut ......... ThOC 11:35-11:50 Oschkinat, Hartmut ...................... Poster 365 Ostrovsky, Dmitry ......................... Poster 100 Ouari, Olivier ................................ Poster 148 Ouari, Olivier ................................ Poster 232 Ouyang, Anli .................... WOB 11:10-11:35 Ovchinnikova, Oxana ................... Poster 335 Oyler, Nathan ............................... Poster 352 Paaske, Berit ................................ Poster 365 Padrta, Petr ........................... TOD 5:35-5:50 Palmer, Melissa ........................... Poster 363 Pan, Duohai ................................. Poster 281 Pan, Duohai ................................. Poster 282 Pang, Xiaodong ........................... Poster 384 Panosyan, Henry ......................... Poster 224 Papernaya, Lyubov ...................... Poster 213 Papouskova, Veronika .......... TOD 5:35-5:50 Paquette, Michelle ....................... Poster 352 Paramasivam, Sivakumar ............ Poster 363 Paravastu, Anant ......................... Poster 384 Paravastu, Anant ......................... Poster 389 Parella, Teodor ............................ Poster 216 Park, Younghee ........................... Poster 039 Parthasarathy, Sudhakar .... TOA 9:50-10:05 Parthasarathy, Sudhakar ............. Poster 078 Parthasarathy, Sudhakar ............. Poster 317 Pastawski, Horacio ...................... Poster 380 Pastawski, Horacio M. ................. Poster 113

INDEX OF AUTHORS


Page 117

Pastawski, Horacio Miguel ...ThOE 4:00-4:25 Patz, Samuel ............................... Poster 147 Paul, Subhradip ........................... Poster 267 Paulsen, Jeffrey ........................... Poster 090 Pauly, Markus .............................. Poster 191 Pawłowska, Monika ..................... Poster 019 Paz, Filipe .................................... Poster 386 Pecharsky, Vitalij K. ..................... Poster 354 Peden, Charles H. F. ........ TOC 12:05-12:20 Pell, Andrew ...................... MOB 11:50-12:05 Pell, Andrew ................................. Poster 374 Pena, Pedro ................................. Poster 058 Peng, Chen ......................ThOB 11:35-11:50 Peng, Jeffrey ................................ Poster 049 Peng, Jeffrey ................................ Poster 255 Perera, Lalith ............................... Poster 071 Perez, Manuel .............................. Poster 302 Perez, Manuel ..................ThOB 11:35-11:50 Peterson, Gregory ....................... Poster 342 Petit, Camille ................................ Poster 342 Petronilho, Elaine ......................... Poster 291 Petzold, Katja ....................... WOD 5:20-5:35 Pflueger, Fred .............................. Poster 062 Pich, Andrij ................................... Poster 110 Pierattelli, Roberta ............ MOB 11:50-12:05 Pileio, Giuseppe ........................... Poster 154 Pileio, Giuseppe ................... WOA 9:20-9:30 Pilger, Jens ...................... WOB 11:35-11:50 Pines, Alex .............................FOA 9:35-9:50 Pines, Alex ................................... Poster 161 Pines, Alex ................................... Poster 018 Pines, Alexander .......................... Poster 124 Pintacuda, Guido ......................... Poster 374 Pintacuda, Guido ............ ThOC 11:35-11:50 Pintacuda, Guido ......................... Poster 315 Pintacuda, Guido .............. MOB 11:50-12:05 Piszczek, Grzegorz ............... TOD 5:05-5:20 Platts, David ................................. Poster 178 Pogorelov, Taras ......................... Poster 009 Polenova, Tatyana ....................... Poster 006 Polenova, Tatyana ....................... Poster 363 Polenova, Tatyana ....................... Poster 045 Polenova, Tatyana ....................... Poster 040 Pondaven, Simon ........................ Poster 193 Pongs, Olaf ..................... ThOC 11:50-12:05 Pöppler, Ann-Christin ................... Poster 220 Porter, Sarah F. ........................... Poster 059 Post, Carol B. ............................... Poster 043 Potapov, Alexey .............. ThOC 11:10-11:35 Potapov, Alexey ........................... Poster 133 Poupon, Cyril ............................... Poster 186 Pourfathi, Mehrdad .............. WOE 5:35-5:50 Pourfathi, Mehrdad ...................... Poster 153 Pourfathi, Mehrdad ...................... Poster 154 Pourfathi, Mehrdad ...................... Poster 156 Pourfathi, Mehrdad ...................... Poster 155 Pourfathi, Mehrdad ...................... Poster 152 Pourpoint, Frederique ........... MOD 5:05-5:20 Powers, Robert ................ WOB 10:45-11:10 Pozhidaeva, Alexandra ................ Poster 061 Pozhidaeva, Alexandra ................ Poster 065 Prakash, Om ................................ Poster 237 Preihs, Christian .......................... Poster 135 Price, William ............................... Poster 097 Procell, Suzanne .......................... Poster 210 Profka, Harrila ...................... WOE 5:35-5:50 Profka, Harrilla ............................. Poster 152 Prusiner, Stanley B. ..................... Poster 018 Pruski, Marek ............................... Poster 354 Pullinger,, Benjamin ..................... Poster 152 Purdie, Jennifer ................ WOB 11:10-11:35

Purusottam, Rudra N. .................. Poster 245 Pustelny, Szymon ........................ Poster 229 Pustovalova, Yulia ....................... Poster 065 Pustovalova, Yulia ....................... Poster 061 Qafoku, Odeta ............................. Poster 344 Qian, Chunqi ................................ Poster 183 Qiang, Wei ................................... Poster 310 Qiang, Wei ...................... ThOC 11:10-11:35 Qingjia, Bao ................................. Poster 077 Qiu, Yujie ..................................... Poster 102 Quiroz, Ryan ......................... TOE 5:35-5:50 Rademacher, Christoph ............... Poster 288 Ragavan, Mukundan .................... Poster 129 Ragavan, Mukundan .................... Poster 131 Raghothama, S. ........................... Poster 052 Rai, Awadhesh K. ........................ Poster 277 Rai, Prashant Kumar .................. Poster 277 Rai, Ratan K. ............................... Poster 327 Rai, Ratan K. ............................... Poster 214 Raman, Steven ............................ Poster 164 Ramaswamy, Vijaykumar ............ Poster 179 Ramaswamy, Vijaykumar ............ Poster 215 Ramaswamy, Vijaykumar ..... MOE 5:05-5:20 Ramirez, Richard M. .................... Poster 161 Ramírez-Cordero, Belen .............. Poster 067 Rao, Timsi .................................... Poster 021 Ratiney, Hélène ................... WOE 4:50-5:05 Ratnakar, S. James ..................... Poster 157 Ratnakar, S. James ..................... Poster 128 Ratnakar, S. James ..................... Poster 135 Reddy, G. Jithender ..................... Poster 200 Reese, Marcel .................. WOB 11:35-11:50 Regatte, Ravinder ........................ Poster 270 Rehage, Heinz ..................... WOE 5:20-5:35 Reidel, Alex R. ............................. Poster 349 Reimer, Jeffrey ............................ Poster 240 Reimer, Jeffrey ................ WOC 10:45-11:10 Reining, Anke ...................... WOD 4:00-4:25 Ren, Xiaobai ................................ Poster 060 Renault, Marie ...................... FOA 8:55-9:20 Resch-Genger, Ute ...................... Poster 348 Resnick, Jesse ............................. Poster 178 Reynaud, Olivier .......................... Poster 186 Ribeiro, Anthony A ....................... Poster 219 Rice, David .................................. Poster 040 Rice, David M. ............................. Poster 326 Ridge, Clark D. ............................ Poster 223 Rienstra, Chad ............................. Poster 328 Rienstra, Chad ............................. Poster 330 Rienstra, Chad ............................. Poster 008 Rienstra, Chad ............................. Poster 009 Rienstra, Chad .................. TOA 09:20-09:35 Rienstra, Chad ............................. Poster 326 Rinnenthal, Jorg ................... WOD 4:00-4:25 Ritz, Emily .................................... Poster 332 Rivera, Edwin ............................... Poster 285 Rivera-Ascona, Christian .... ThOE 4:25-4:50 Rizi, Rahim .................................. Poster 153 Rizi, Rahim .................................. Poster 152 Rizi, Rahim .................................. Poster 156 Rizi, Rahim R. .............................. Poster 155 Rizi, Rahim R. .............................. Poster 154 Rizi, Rahim R. ...................... WOE 5:35-5:50 Rizzato, Egon .............................. Poster 232 Roach, David ............................... Poster 346 Rocha, Gustavo ........................... Poster 291 Rocha, João ................................. Poster 388 Rodríguez, Alberto ....................... Poster 208 Rogov, Vladimir ........................... Poster 197 Roiland, Claire ............................. Poster 347 Romalis, Michael V. ..................... Poster 138

Rommereim, Don ......................... Poster 114 Ronk, Mike ................................... Poster 252 Rosas, Roselyne .......................... Poster 232 Rosay, Melanie M. ....................... Poster 325 Rosay, Melanie M. ....................... Poster 148 Rosay, Melanie M. ....................... Poster 132 Rosen, Matthew ............... WOC 11:35-11:50 Rosen, Matthew ........................... Poster 147 Rosenberry, Terrone .................... Poster 389 Rosenman, David ........................ Poster 279 Rossin, Joseph ............................ Poster 342 Rossini, Aaron J. .......................... Poster 148 Rößler, Ernst ................................ Poster 146 Rosso, Kevin ....................... ThOD 5:35-5:50 Rostovtseva, Tatiana ........ MOB 12:05-12:20 Roussel, Tangui ................... WOE 4:50-5:05 Rovnyak, David ............................ Poster 363 Rozenknop, Alexis ....................... Poster 197 Ruan, Ke ...................................... Poster 294 Rusakov, Yury .............................. Poster 213 Ryabov, Yaroslav .................. TOD 5:20-5:35 Ryan, Herbert ............................... Poster 182 Sachleben, Joseph ...................... Poster 205 Sahakyan, Aleksandr ................... Poster 224 Sakellariou, Dimitrios .......... FOA 9:50-10:05 Saksouk, Nehme .......................... Poster 058 Salazar, Andre ............................. Poster 322 Saleem, Qasim ............................ Poster 314 Salmon, Loic ................................ Poster 112 Salvi, Nicola .................... ThOB 12:02-12:20 Samoson, Ago ............................. Poster 357 Sánchez, Claudia Marina .... ThOE 4:00-4:25 Sánchez-Pedregal, Victor WOB 11:35-11:50 Sanderova, Hana .................. TOD 5:35-5:50 Sanders, Kevin ............................. Poster 272 Sanders, Kevin J. ......................... Poster 343 Sandin, Henrik ............................. Poster 087 Sant'Anna, Ricardo ...................... Poster 030 Santos, Sérgio ............................. Poster 386 Santos, Sérgio M. ........................ Poster 388 Santos De Freitas, Mônica........... Poster 030 Sardo, Mariana ............................ Poster 388 Sarkar, Riddhiman ............... WOA 8:55-9:20 Sarkar, Riddhiman ........... WOC 12:05-12:20 Sarzedas, Carolina ...................... Poster 192 Sasaki, Ryan R. ........................... Poster 300 Sasaki, Ryan R. ........................... Poster 286 Satchell, Karla .............................. Poster 008 Satterfield, Emmalou .................... Poster 222 Saurí, Josep ................................. Poster 216 Sawicki, Janet A. .................. WOE 5:35-5:50 Schaefer, Hartmut ........... ThOB 11:10-11:35 Scheler, Ulrich .............................. Poster 235 Schieber, Loren ............................ Poster 387 Schiffer, Alexander........... WOB 11:35-11:50 Schimpf, Rémy ...................... MOE 4:50-5:05 Schmidt, Christopher ............ TOD 4:50-5:05 Schmidt, Christopher ................... Poster 076 Schnakenberg, Uwe..................... Poster 174 Schneider, Celine ......................... Poster 338 Schneider, Robert ........... ThOC 11:35-11:50 Schuetz, Anne .............................. Poster 335 Schuetz, Birk ................... ThOB 11:10-11:35 Schurko, Robert W. ...................... Poster 350 Schurko, Robert W. .............. MOD 5:35-5:50 Schurko, Robert W. ...................... Poster 349 Schwalbe, Harald ................. WOD 4:00-4:25 Schwieters, Charles D. ................ Poster 006 Schwieters, Charles D. ................ Poster 084 Schwieters, Charles D. ....... ThOD 5:20-5:35 Schwieters, Charles D. ......... TOA 9:20-9:35

INDEX OF AUTHORS


Page 118

Schwieters, Charles D. ......... TOD 5:20-5:35 Schwieters, Charles D. ......FOB 11:10-11:35 Scott, Eric .................................... Poster 240 Sears, Jesse A. ............................ Poster 114 Sears, Jesse A. ................. TOC 12:05-12:20 Sears, Jesse A. ................... ThOD 5:35-5:50 Segawa, Takuya .................. WOA 8:55-9:20 Sekar, Giridhar ............................. Poster 131 Sekar, Giridhar ............................. Poster 129 Seltzer, Scott ............................... Poster 124 Seltzer, Scott .........................FOA 9:35-9:50 Sen, Sabyasachi .......................... Poster 369 Sengupta, Ishita .................... MOD 5:20-5:35 Sengupta, Suvrajit ....................... Poster 189 Senker, Juergen .......................... Poster 146 Seoane, Felipe ............................. Poster 302 Seoane, Felipe ............................. Poster 304 Sesanker, Colbert ........................ Poster 301 Sessler, Jonathan L ..................... Poster 135 Sesti, Erika ............................ MOE 4:00-4:25 Seto, Haruo .................................. Poster 209 Sgourakis, Nikolaos ............ ThOD 5:05-5:20 Shaffer, David V. .......................... Poster 161 Shaghaghi, Hoora ................ WOE 5:35-5:50 Shah, Anup .................................. Poster 063 Shahkhatuni, Aleksan .................. Poster 224 Shahkhatuni, Astghik ................... Poster 224 Shapiro, Mikhail G. ...................... Poster 161 Sharma, Gaurav .......................... Poster 293 Sharma, Gaurav .......................... Poster 277 Shatrova, Alexandra .................... Poster 213 Shchepin, Roman ........................ Poster 145 Shchepin, Roman ........................ Poster 140 Shealy, Paul ................................. Poster 073 Shen, Bo ...................................... Poster 252 Shen, Clifton ..........................TOE 5:35-5:50 Sheppard, Devon ......................... Poster 038 Sheriff, Sulaiman ......................... Poster 248 Sherry, A. Dean ........................... Poster 135 Sherry, A. Dean ........................... Poster 157 Sheveleva, Nadezhda .................. Poster 324 Shi, Junhui ................................... Poster 138 Shi, Lichi ...................................... Poster 334 Shi, Lichi ...................................... Poster 332 Shi, Xiangyan ............................... Poster 036 Shimizu, Linda S .......................... Poster 130 Shin, Chang ................................. Poster 124 Shin, Hyun Doug ....................FOA 9:35-9:50 Sholl, David .................................. Poster 109 Showalter, Scott ........................... Poster 198 Shu, Jie ........................................ Poster 079 Shukla, Matsyendra Nath ............ Poster 089 Siaw, Ting Ann ............................. Poster 142 Siegel, Renée .............................. Poster 386 Siegel, Renée .............................. Poster 388 Sifuentes, Roxana ....................... Poster 212 Silva De Paula, Viviane ............... Poster 050 Silva Elipe, Maria Victoria ............ Poster 252 Simin, Mikhail ............................... Poster 082 Simin, Mikhail ........................ TOD 4:50-5:05 Simin, Mikhail ............................... Poster 073 Simplaceanu, Virgil ...................... Poster 064 Simpson, Andre J. ....................... Poster 231 Simpson, Andre J. ....................... Poster 221 Simpson, Andre J. ....................... Poster 207 Simpson, Andre J. ........... WOC 11:50-12:05 Simpson, Andre J. ....................... Poster 360 Simpson, Andre J. ....................... Poster 247 Simpson, Andre J. ....................... Poster 123 Simpson, Myrna J. ....................... Poster 360 Simpson, Myrna J. ........... WOC 11:50-12:05

Singh, Chandan ........................... Poster 327 Singh, Niraj K. .............................. Poster 354 Sinha, Neeraj ............................... Poster 214 Sinha, Neeraj ............................... Poster 327 Sinha, Neeraj ............................... Poster 245 Sirigiri, Jagadishwar ..................... Poster 171 Sitkowski, Jerzy ........................... Poster 217 Sitkowski, Jerzy ........................... Poster 020 Sitkowski, Jerzy ........................... Poster 019 Sivanandam, V. N. ....................... Poster 049 Sivanandam, V. N. ....................... Poster 336 Skemer, Philip .............................. Poster 340 Sklenar, Vladimir ................... TOD 5:35-5:50 Sklenar, Vladimir .......................... Poster 003 Skrynnikov, Nikolai R. .................. Poster 256 Skrynnikov, Nikolai R. .......... WOD 5:05-5:20 Skrynnikov, Nikolai R. .................. Poster 043 Smirnov, Alex I. ............................ Poster 378 Smit, Berend ................................ Poster 240 Smith, Adam ................................ Poster 307 Smith, Albert ................................ Poster 127 Smith, Albert ................................ Poster 150 Smith, Albert ................................ Poster 144 Smith, Steven ....................... TOD 4:00-4:25 Smitka, Tim ...................... WOB 11:10-11:35 Soares, Sibelle ............................. Poster 291 Song, Yi-Qiao .............................. Poster 176 Song, Yi-Qiao .............................. Poster 172 Song, Yi-Qiao .............................. Poster 173 Song, Yi-Qiao .............................. Poster 090 Song, Yi-Qiao .............................. Poster 187 Song, Youngkyu .......................... Poster 090 Sonkar, Kanchan ......................... Poster 245 Soong, Ronald ................. WOC 11:50-12:05 Soong, Ronald ............................. Poster 360 Soong, Ronald ............................. Poster 231 Soong, Ronald ............................. Poster 207 Soong, Ronald ............................. Poster 247 Soong, Ronald ............................. Poster 123 Sorce, Dennis ....................... TOE 5:20-5:35 Sorce, Dennis .............................. Poster 101 Sordo, Maruxa ............................. Poster 302 Sperling, Lindsay J. ..................... Poster 018 Sperling, Lindsay J. ..................... Poster 161 Sperling, Lindsay J. .............. TOA 9:20-9:35 Spiess, Hans ................................ Poster 386 Spiess, Hans W. .................. WOA 8:30-8:55 Spiess, Hans Wolfgang ............... Poster 079 Spraul, Manfred .............. ThOB 11:10-11:35 Srnec, Matthew ............................ Poster 336 Stanton, Christopher ............. MOE 4:00-4:25 Stec, Donald ................................ Poster 095 Stein, Paul C. ........................ MOE 4:50-5:05 Steinert, Hannah .................. WOD 4:00-4:25 Stewart, Mikaela .......................... Poster 257 Stockmann, Jason ....................... Poster 258 Stöhr, Jan .................................... Poster 018 Stone, Michael ............................. Poster 054 Stoyanova, Radostina .................. Poster 357 Strobridge, Fiona ......................... Poster 374 Stronks, Henry J. ......................... Poster 123 Stronks, Henry J. ............. WOC 11:50-12:05 Struppe, Jochem .......................... Poster 312 Struppe, Jochem .......................... Poster 123 Struppe, Jochem .............. WOC 11:50-12:05 Stueber, Dirk ................................ Poster 295 Su, Yongchao ................... MOB 12:05-12:20 Su, Yongchao .............................. Poster 319 Subramanian, Vivekanandan ....... Poster 288 Suiter, Christopher ....................... Poster 040 Suiter, Christopher ....................... Poster 045

Suiter, Christopher ....................... Poster 363 Sun, Cheng .................................. Poster 375 Sun, George ................................. Poster 161 Sun, Jinny .................................... Poster 161 Sun, Peng .................................... Poster 283 Sun, Shangjin ............................... Poster 363 Sun, Shangjin ............................... Poster 190 Sun, Xiuzhi ................................... Poster 237 Sun, Ying ..................................... Poster 168 Surface, J. Andrew ....................... Poster 340 Susmitha, A. L. ............................. Poster 226 Suter, Dieter ......................... WOE 5:20-5:35 Swager, Timothy .......................... Poster 127 Swager, Timothy .......................... Poster 150 Swager, Timothy M. ..................... Poster 141 Swartz, Harold ............................. Poster 085 Sykora, Stanislav ......................... Poster 302 Sykora, Stanislav ......................... Poster 304 Sykora, Stanislav .................. FOA 9:20-9:35 Sykora, Stanislav ............ ThOB 11:50-12:05 Szejnfeld, Jacob ........................... Poster 243 Szulik, Marta ................................ Poster 054 Tajkhorshid, Emad ....................... Poster 009 Tam, Leo ...................................... Poster 258 Tang, Huiru ..................... ThOB 10:45-11:10 Tang, Huiru .................................. Poster 250 Tang, Joel A. ..................... TOC 11:35-11:50 Tang, Joel A. ......................... MOE 5:20-5:35 Tang, Ming ............................ TOA 9:20-9:35 Tang, Ming ................................... Poster 326 Tang, Wenxing ............................. Poster 378 Tanokura, Masaru ........................ Poster 254 Tarasek, Matthew ............... ThOD 4:25-4:50 Tars, Kaspars .................. ThOC 11:35-11:50 Tashiro, Mitsuru ........................... Poster 209 Tata, Gopinath ................ ThOC 12:05-12:20 Tata, Gopinath ............................. Poster 321 Taulelle, Francis ........................... Poster 268 Taulelle, Francis ........................... Poster 379 Tay, William ................................. Poster 389 Tayler, Michael ..................... WOA 9:20-9:30 Tayyari, Fariba ............................. Poster 253 Tejchman-Małecka, Bożena ........ Poster 019 Teles, Joao ......................... ThOE 4:25-4:50 Temkin, Richard ........................... Poster 180 Temkin, Richard ........................... Poster 188 Temkin, Richard J. ............ FOB 11:50-12:05 Thakkar, Ajay ............................... Poster 188 Thakkar, Ajay .................... FOB 11:50-12:05 Thévand, André ........................... Poster 091 Thiele, Christina M. ...................... Poster 206 Thomas, M. Albert ........................ Poster 164 Thurber, Kent .................. ThOC 11:10-11:35 Thurber, Kent ............................... Poster 133 Thureau, Pierre ............................ Poster 373 Thureau, Pierre ............................ Poster 091 Tian, Changlin .............................. Poster 165 Tikole, Suhas ............................... Poster 072 Tikole, Suhas ............................... Poster 197 Tinoco, Luzineide ......................... Poster 192 Tishchenko, Evgeny..................... Poster 015 Tjandra, Nico ..................... FOB 11:10-11:35 Tjandra, Nico ......................... TOD 5:05-5:20 Tobias, Douglas ........................... Poster 004 Tochio, Hidehito ........................... Poster 007 Toda, Mitsuru ..................... WOA 9:50-10:05 Tolman, Joel R ............................. Poster 194 Tommassen, Jan .................. FOA 8:55-9:20 Tommassen-van Boxtel, Ria .............................................. FOA 8:55-9:20 Tonelli, Marco .............................. Poster 059

INDEX OF AUTHORS


Page 119

Tonyushkin, Alexey ...................... Poster 119 Torchia, Dennis ................. MOB 11:35-11:50 Tordo, Paul .................................. Poster 148 Tordo, Paul .................................. Poster 232 Torresani, Bruno .......................... Poster 241 Toumi, Ichrak ............................... Poster 241 Tozoni, Jose R. ....................ThOE 4:25-4:50 Traaseth, Nathaniel J .........FOB 12:05-12:30 Trease, David .............................. Poster 124 Trease, Nicole ......................ThOA 9:35-9:50 Trebosc, Julien ............................ Poster 367 Trebosc, Julien ............................ Poster 268 Trebosc, Julien ............................ Poster 379 Trebosc, Julien ............................ Poster 132 Trébosc, Julien ............................ Poster 371 Trigo-Mouriño, Pablo ................... Poster 212 Truong, Milton .............................. Poster 145 Tucker, Don ................................. Poster 086 Tugarinov, Vitali ........................... Poster 203 Tuherm, Tiit .................................. Poster 357 Turcu, Flaviu ................................ Poster 114 Turcu, Flaviu ....................... ThOD 5:35-5:50 Turovets, Sergei .......................... Poster 086 Turro, Nicholas J. ............. WOC 12:05-12:20 Tuttle, Marcus .............................. Poster 328 Twomey, Edward ......................... Poster 069 Tyan, Andrew .........................TOE 5:20-5:35 Tycko, Robert ................. ThOC 11:10-11:35 Tycko, Robert .............................. Poster 310 Tycko, Robert .............................. Poster 133 Tyukhtenko, Sergiy ...................... Poster 023 Ueda, Keisuke ................... WOA 9:50-10:05 Ukpebor, Obehi ............................ Poster 063 Ulijasz, Andrew T. ........................ Poster 033 Ullah, Mukta ................................. Poster 058 Ulmer, Stefan .........................FOA 8:30-8:55 Un, Ilker ....................................... Poster 276 Urbaitis, Algis ............................... Poster 086 Utsuzawa, Shin ............................ Poster 172 Vaara, Juha ................................. Poster 138 Valafar, Homayoun ............... TOD 4:50-5:05 Valafar, Homayoun ...................... Poster 073 Valafar, Homayoun ...................... Poster 076 Valafar, Homayoun ...................... Poster 082 Valente, Ana Paula ...................... Poster 050 van Bentum, Jan .......................... Poster 159 van Bentum, Jan .......................... Poster 359 van Criekinge, Mark ..................... Poster 139 van Criekinge, Mark ..................... Poster 134 van der Heijden, Gijs ................... Poster 159 van der Wel, Patrick .......... MOB 12:05-12:20 van der Wel, Patrick C. A. ............ Poster 336 van der Wel, Patrick C. A. ............ Poster 323 van Eck, Ernst .............................. Poster 351 van Ingen, Hugo .......................... Poster 288 van Zijl, Peter .........................TOE 5:05-5:20 Vanarotti, Murugendra ................. Poster 026 Vanni, Julieann ............................ Poster 037 Varga, Krisztina ........................... Poster 326 Vasenkov, Sergey ........................ Poster 130 Vasenkov, Sergey ........................ Poster 109 Vaz, Esther .................................. Poster 302 Veera Mohan Rao, K. .................. Poster 218 Veera Mohan Rao, K. .................. Poster 383 Veglia, Gianluigi .............. ThOC 12:05-12:20 Veglia, Gianluigi .................FOB 12:05-12:30 Veglia, Gianluigi ........................... Poster 066 Veglia, Gianluigi ........................... Poster 321 Veloro, Angelo ............................. Poster 032 Velpandian, Thirumurty ................ Poster 293 Vendruscolo Michele ........ThOD 4:00 – 4:25

Verardi, Raffaello .............. FOB 12:05-12:30 Vezin, Herve ................................ Poster 132 Vicente, Aurélie ............................ Poster 264 Vidal, Thaís .................................. Poster 192 Vidoto, Edson L. G. ............. ThOE 4:25-4:50 Viel, Stéphane ............................. Poster 232 Viel, Stéphane ............................. Poster 091 Vierstra, Richard D. ..................... Poster 033 Vigneron, Daniel B. ...................... Poster 139 Vingara, Lisa ................................ Poster 246 Vinther, Joachim M. ..................... Poster 362 Vitzthum, Veronika ....................... Poster 371 Vold, Robert L. ............................. Poster 100 Volden, Paul ................................ Poster 205 Volegov, Petr ............................... Poster 087 Volegov, Petr ............................... Poster 086 Vosegaard, Thomas .................... Poster 299 Vranken, Wim .............................. Poster 071 Vugmeyster, Liliya ....................... Poster 100 Vyas, Jay ..................................... Poster 301 Wacker, Anna ...................... WOD 4:00-4:25 Waddell, Kevin ............................. Poster 140 Waddell, Kevin ............................. Poster 145 Wagner, Dominik ................. WOD 4:00-4:25 Wagner, George W. ..................... Poster 342 Wagner, Gerhard ......................... Poster 025 Wagner, Gerhard ................. WOA 9:35-9:50 Wagner, Gerhard ......................... Poster 199 Wagner, Gerhard ......................... Poster 196 Wagner, Gerhard .............. MOB 12:05-12:20 Wald, Larry ........................... TOE 4:25-4:50 Walder, Brennan .......................... Poster 364 Walder, Brennan .......................... Poster 272 Walish, Joseph J. ......................... Poster 141 Walker, Joseph M. ....................... Poster 033 Walker, Shamon .......................... Poster 142 Walkup, Laura L. .......................... Poster 147 Walls, Jamie ................................ Poster 223 Walls, Jamie ................................ Poster 230 Walsworth, Ronald ........... WOC 11:35-11:50 Walter, Eric .................................. Poster 114 Wand, Joshua .............................. Poster 201 Wand, Joshua ...................... WOD 4:50-5:05 Wang, Chunyu ............................. Poster 279 Wang, Shenlin ............................. Poster 334 Wang, Songlin ............................. Poster 313 Wang, Tongtong .............. WOB 11:10-11:35 Wang, Tuo ................................... Poster 320 Wang, Tuo ................................... Poster 322 Wang, Tuo ................................... Poster 308 Wang, Wen-Tung ......................... Poster 169 Wang, Xingsheng ........................ Poster 255 Wang, Yao ................................... Poster 315 Wang, Yong ...................... TOC 12:05-12:20 Wang, Yu .......................... FOB 11:10-11:35 Wang, Yulan ................... ThOB 10:45-11:10 Wang, Yunlan .............................. Poster 250 Warnet, Xavier ............................. Poster 311 Warren, Warren S. ............... WOE 4:25-4:50 Warschawski, Dror E. .................. Poster 311 Washton, Nancy .......................... Poster 114 Wasmer, Christian ....................... Poster 025 Watal, Geeta ................................ Poster 277 Watanabe, Miki ............................ Poster 248 Watzlaw, Jan ............................... Poster 174 Weatherby, Gerard ...................... Poster 301 Wegner, Martin ............................ Poster 079 Wegstroth, Melanie .......... WOB 11:35-11:50 Wei, Feifei .................................... Poster 254 Wei, Hong .................................... Poster 250 Wei, Yufeng ................................. Poster 069

Weingarth, Markus .......... ThOC 11:50-12:05 Weinhold, Frank ........................... Poster 074 Weliky, David ............................... Poster 366 Wemmer, David E. ....................... Poster 018 Wendt, Ulrich ................... WOB 11:35-11:50 Westler, William M. ...................... Poster 074 Wetzel, Ronald ............................. Poster 323 Wheeler, Dustin .................... MOE 4:00-4:25 Whiting, Nicholas ......................... Poster 147 Whiting, Nicholas ......................... Poster 162 Whittier, Sean .............................. Poster 028 Wi, Sungsool ................................ Poster 341 Wilczek, Marcin ............................ Poster 273 Wille, Holger ................................. Poster 018 Williams, Benjamin ....................... Poster 085 Williams, John .............................. Poster 006 Williamson, Philip T.......... WOC 12:05-12:20 Williamson, Philip T.F. ................. Poster 002 Wilson, Brenda ............................. Poster 008 Wilson, Brian ................................ Poster 049 Wilson, David ............................... Poster 134 Wilson, David M. .......................... Poster 139 Wilson, Kimberly .......................... Poster 255 Wilson, Neil .................................. Poster 164 Wilson, Samuel ............................ Poster 010 Withers, Richard .......................... Poster 179 Withers, Richard ................... MOE 5:05-5:20 Withers, Richard .......................... Poster 215 Woelk, Klaus ................................ Poster 225 Woelk, Klaus ................................ Poster 372 Wolff, Marc ................................... Poster 274 Wong, Dana ................................. Poster 250 Worthoff, Wieland ................. MOE 4:00-4:25 Woskov, Paul ............................... Poster 188 Wrachtrup, Jorg .................. ThOA 8:55-9:20 Wu, Bainan .................................. Poster 280 Wu, Chin H. .................................. Poster 115 Wu, Chin H. .................................. Poster 175 Wu, Jian ....................................... Poster 234 Wu, Kuen-Phon ............................ Poster 031 Wu, Zhen ..................................... Poster 358 Wu, Zhen ..................................... Poster 356 Wuerth, Christian ......................... Poster 348 Wuttke, Deborah .......................... Poster 021 Wylie, Benjamin J ........... ThOC 10:45-11:10 Xiao, Yiling ................................... Poster 317 Xie, Li ........................................... Poster 366 Xu, Dian ....................................... Poster 167 Xu, Xiang .............................. MOE 5:20-5:35 Xue, Yi ......................................... Poster 256 Xue, Yi ................................. WOD 5:05-5:20 Yaghi, Omar ................................. Poster 240 Yan, Fangyong ............................. Poster 240 Yan, Si ......................................... Poster 006 Yang, Chen .................................. Poster 312 Yang, Guang ................................ Poster 347 Yang, Ming ............................ TOE 5:05-5:20 Yang, Shan .................................. Poster 112 Yang, Shan .................................. Poster 042 Yang, Xiang-Jiao .......................... Poster 058 Yang, Yifeng .................... WOC 12:05-12:20 Yang, Yuan .................................. Poster 092 Yang, Yunhuang .......................... Poster 053 Yao, Hongwei ............................... Poster 308 Yap, Thai Leong ........................... Poster 044 Yarger, Jeffery L. ......................... Poster 167 Yarger, Jeffery L. ......................... Poster 036 Yasuoka, Hiroshi .......................... Poster 239 Yau, Wai-Ming ............................. Poster 133 Yau, Wai-Ming ................ ThOC 11:10-11:35 Ye, Chaohui ................................. Poster 143

INDEX OF AUTHORS


Page 120

Ye, Weihua .................................. Poster 195 Yeung, Kelvin W. K. ..................... Poster 250 Yi, Ruiyang .................................. Poster 205 Yin, Shawn ................................... Poster 281 Ying, Jinfa ......................... MOB 11:35-11:50 Yu, Bingwu ....................... WOB 11:50-12:05 Yu, Bingwu ................................... Poster 288 Yu, Liping ..................................... Poster 024 Yu, Tao ..................................TOE 5:05-5:20 Yuan, Yue .................................... Poster 064 Yucelen, Ipek ............................... Poster 109 Yuwen, Tairan .............................. Poster 256 Yuwen, Tairan .............................. Poster 043 Zabotina, Olga ............................. Poster 322 Zagdoun, Alexandre .................... Poster 148 Zanca, Michel ....................... MOE 4:50-5:05 Zang, Ji ........................................ Poster 109 Zangara, Pablo R. ........................ Poster 113 Zapletal, Vojtech .......................... Poster 003

Zelenova, Yelena ......................... Poster 376 Zeng, Haifeng .............................. Poster 131 Zeng, Haifeng .................. WOB 11:35-11:50 Zhang, Boyang ..................... MOE 5:20-5:35 Zhang, Boyang ............... ThOA 09:50-10:05 Zhang, Fengli ............................... Poster 244 Zhang, Tianlan ............................. Poster 234 Zhang, Wurong ............................ Poster 177 Zhang, Xiaolu .................. ThOB 11:35-11:50 Zhang, Xu .................................... Poster 283 Zhang, Yanli ................................. Poster 016 Zhang, Yonghong ........................ Poster 263 Zhang, Yuan ................................ Poster 319 Zhang, Zhiyang ................. TOC 11:50-12:05 Zhang, Zhiyang ............................ Poster 236 Zharavin, Victor ............................ Poster 197 Zharavin, Victor ............................ Poster 072 Zhong, Guiming ................ TOC 11:35-11:50 Zhou, Ben .................................... Poster 374

Zhou, Donghua H. ........................ Poster 368 Zhou, Huan-Xiang ........................ Poster 384 Zhou, Jun ..................................... Poster 385 Zhou, Xin ...................................... Poster 143 Zhu, Gang .................................... Poster 090 Zhu, Kake .......................... TOC 12:05-12:20 Zhu, Liu ........................................ Poster 105 Zhu, Peizhi ................................... Poster 309 Zhu, Siqi ....................................... Poster 108 Ziarek, Joshua ............................. Poster 278 Zidek, Lukas ................................. Poster 003 Zidek, Lukas .......................... TOD 5:35-5:50 Zilm, Kurt ........................... TOB 11:20-12:25 Zilm, Kurt W. ................................ Poster 189 Zimmerman, Max ......................... Poster 384 Zou, Xiaowei ................................ Poster 098 Zvonok, Nikolai ............................ Poster 023

DIRECTORY OF PARTICIPANTS

Page 121

Ralph Adams University of Manchester School of Chemistry Oxford Road Manchester, M13 9PL UK Tel: +44 (0) 161 2754669 [email protected]

Chris Akel

University of Florida 6519 W Newberry Rd., Unit B6 Gainesville, FL 32605 [email protected]

Serge Akoka

CEISAM, UMR 6230, CNRS/Univ de Nantes UFR Sciences - 2 rue de la houssiniere BP 92208 Nantes, Pays de la Loire 44322 France Tel: (33) 251125707 [email protected]

Lawrence B. Alemany

Rice University Department of Chemistry, MS-60 Houston, TX 77005 Tel: 713-348-5360 [email protected]

Charlie Alexander

Triangle Analytical, Inc. 101 Pheasant Wood Ct Morrisville, NC 24560 Tel: 919 461 2300 [email protected]

Fabio Almeida

UFRJ Av. Carlos Chagas Filho, 373 - CCS - Bloco K Anexo Rua Viriato Correa, 91 casa Rio de Janeiro, Rio de Janeiro 21941-902 Brazil Tel: 5521-31042326 [email protected]

Jean Paul Amoureux

Lille niversity UCCS Building C7 Villeneuve d'Ascq, France 59652 France Tel: (33) 320434143 [email protected]

Takahiro Anai

JEOL 1-2 MUSASHINO 3-CHOME AKISIMA TOKYO, 196-8558 Japan [email protected]

Kathleen Anderson

Agilent Technologies 3501 Stevens Creek Blvd Santa Clara, CA 95051 [email protected]

Loren Andreas

Massachusetts Institute of Technology 150 Albany St. Building NW14-4121 Cambridge, MA 02142 [email protected]

Maria Andreu Triangle Analytical 101 Pheasant Wood Court Morrisville, NC 27560 [email protected]

Cristina Angelo

Isotec 3858 Benner Rd Miamisburg, OH 45342 Tel: 937-859-1808 [email protected]

Clemens Anklin

Bruker BioSpin 15 Fortune Drive Billerica, MA 01821 Tel: 978 667 9580 [email protected]

Nelly Aranibar

Bristol-Myers Squibb P.O. Box 4000 Princeton, NJ 8543 Tel: (609)2524541 [email protected]

Luke Arbogast

The Johns Hopkins University 3400 N. Charles St Remsen 229A Baltimore, MD 21218 Tel: 804-363-2993 [email protected]

Jan Henrik Ardenkjaer-Larsen

GE Healthcare Asmussens Alle 1, 3th Frederiksberg, 1808 Denmark jan.henrik.ardenkjaerâ € [email protected]

Armando Ariza-Castolo

Cinvestav-IPN, Department of Chemistry Av. IPN 2508, Zacatenco Mexico D.F., Distrito Federal 7360 Mexico Tel: (+52-55)57473727 [email protected]

Geoffrey S Armstrong

University of Colorado Dept. of Chemistry and Biochemistry, UCB215 Boulder, CO 80309 Tel: 303-724-3331 [email protected]

Sengodagounder Arumugam

JG Brown Cancer Ctr, Univ of Louisville 529 S. Jackson St. NMR suite, MIRC Louisville, KY 40202 Tel: (502)562-6832 [email protected]

Katsuo Asakura

JEOL Ltd. 3-2-1 Musashino Akishima Tokyo, Asia 196-8558 Japan [email protected]

Atsushi Asano National Defense Academy 1-10-20 Hashirimizu Yokosuka, Kanagawa 2398686 Japan Tel: -4688413729 [email protected]

Sabrina Asher

Wilmad-LabGlass 1172 NW BLVD Vineland, NJ 8360 Tel: 856 691 3200 [email protected]

Jun Ashida

Agilent Technologies 5-6-17-501 Akemi Urayasu, 279-0014 Japan [email protected]

Robert Austin

Field Forensics 7887 Bryan Dairy Road, Ste 510 Largo, FL 33777 Tel: 727 4903609 X113 [email protected]

Hugo F Azurmendi

Virginia Tech Department of Chemistry 006 Hahn Hall Blacksburg, VA 24061 Tel: 540 231 8256 [email protected]

David Badger

USF 4202 E Fowler Ave, CHE205 Tampa, FL 33620 Tel: 614-906-0873 [email protected]

Vlad Badilita

University of Freiburg Dept of Microsystems Engineering â€“ IMTEK Freiburg im Breisgau, 79110 Germany Tel: 4.9761203744e+011 [email protected]

Daryl Baer

Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CA 95051 Tel: 650 424 4962 [email protected]

Scott Baggett

3212 Mecartney Road Alameda, CA 94502 Tel: 5108546259 [email protected]

Guoyun Bai

Pfizer Inc 585 Eastern Point Rd Groton, CT 06340 [email protected]


Page 122

Alex D. Bain McMaster University Dept. of Chemistry 1280 Main St. W. Hamilton, ON L8S 4M1 Canada Tel: 905 525 9140 xt 24524 [email protected]

Vikram S. Bajaj

UC Berkeley and LBNL 208C Stanley Hall Berkeley, CA 94720 Tel: 510-642-7717 [email protected]

Andreea Cristina Balaceanu

DWI an der RWTH Aachen Forckenbeckstr. 50 Aachen, NWR 52056 Germany Tel: ++49 241 80-233-88 [email protected]

Marc Baldus

Utrecht University Bijvoet Center for Biomolecular Research Padualaan 8 Utrecht, Utrecht 3584 CH Netherlands Tel: 31302533801 [email protected]

Gabor Balogh

Gedeon Richter Plc. Gyomroi ut 19-21 Budapest, 1103 Hungary Tel: +36 1 4315388 [email protected]

Jay H Baltisberger

Berea College CPO 1722 Chemistry Department Berea, KY 40404 Tel: 859-985-3298 [email protected]

David Ban

MPI-BPC Max Planck Institute for biophysical Chemistry Am Faßberg 11, Dept of NMR-based Structural Biology Gottingen, Niedersachsen 37077 Germany Tel: 49 551 201-2250 [email protected]

Emeline Barbet-Massin

CRMN / ENS Lyon 5 rue de la Doua Villeurbanne, 69100 France Tel: 33426233868 [email protected]

Alexander Barnes

Massachusetts Institute of Technology 170 Albany St. Cambridge, MA 02139 Tel: 6176423225 [email protected]

Daniel Bernhard Baumann Bruker-Biospin AG Industriestr. 26 Faellanden, 8117 Switzerland Tel: +41 44 825 92 45 [email protected]

Ad Bax

NIH 5 Center Dr., Bldg 5, Rm 126 Bethesda, MD 20892-0520 Tel: 301 402 0907 [email protected]

Maïwenn Beaugrand

Universite du Quebec a Montreal C.P. 8888, Succ. Centre-Ville Montreal, QC H3C 3P8 Canada Tel: 514 987 3000 #4391 [email protected]

Ted Becker

NIH Bethesda, MD [email protected]

Elzbieta Bednarek

National Medicines Institute Chelmska 30/34 Warsaw, 00-725 Poland Tel: +48 22 8514372 [email protected]

Alain Belguise

Bruker Biospin 34 Rue de l'Industrie, BP 10002 Wissembourg Cedex, 67166 France Tel: 0033 3 88 68 45 [email protected]

George M Benedikt

The Lubrizol Corporation 9911 Brecksville Rd Brecksville, OH 44141-3247 Tel: 216-447-5448 [email protected]

Konstantin Berlin

University of Maryland Center for Biomolecular Structure and Organization University of Maryland College Park, MD 20854 [email protected]

Guillermo Bermejo

National Institutes of Health 12 South Drive, Room 2041 Bethesda, MD 20892 Tel: 301-594-5831 [email protected]

Wolfgang Bermel

Bruker BioSpin Silberstreifen Rheinstetten, DE-76287 Germany Tel: +49 721 5161 6119 [email protected]

Bob Berno McMaster University 1280 Main St. West Department of Chemistry Hamilton, ON L8S 4M1 Canada Tel: 905-525-9140 X24158 [email protected]

Michael Bernstein

Mestrelab Research Felicano Barrera Fernanded 9B-BAIXO Santiago de Compostela, Courna 15706 Spain Tel: 34 88 197 6775 [email protected]

Jagadeesh Bharatam

Centre for NMR, Indian Institute of Chemical Techn Tarnaka Hyderabad, AP 500 007 India Tel: 0091-40-2719 3006 , [email protected]

Hrishikesh Bhase

University of Florida B8 NPB Gainesville, FL 32611 [email protected]

Terri Bishop

SP Scientific 3538 Main Street Stone Ridge, NY 12484 Tel: 845 255 5000 [email protected]

Ronald Block

Nova Southeastern Univ. 3200 South University Drive Fort Lauderdale, FL 33328 Tel: 954 262-1319 [email protected]

Benjamin G Bobay

North Carolina State University Dept Molecular and Structural Biochemistry 128 Polk Hall Box 7622 Raleigh, NC 27695 Tel: 919-513-4347 [email protected]

Wojciech Bocian

National Medicines Institute Chelmska 30/34 Warsaw, 00-725 Poland Tel: 48 22 8514372 [email protected]

David Boehr

Penn State 240 Chemistry Building Dept of Chemistry University Park, PA 16802 [email protected]


Page 123

Tito J. Bonagamba IFSC - USP PO Box 369 Sao Carlos, Sao Paulo 13560-970 Brazil Tel: 55 16 3373 9871 [email protected]

Aurélien Bornet

EPFL EPFL SB ISIC LRMB BCH 1533 VD CH-1015 Lausanne Switzerland [email protected]

Arezue Boroujerdi

Claflin University 400 Magnolia St. Orangebug, SC 29115 Tel: 8035355536 [email protected]

Stephanie Bosco

New Era Enterprises PO Box 747 Vineland, NJ 08362-0747 Tel: 856 794 2005 [email protected]

Mark Bostock

University of Cambridge, Department of Biochemistr Selwyn College Cambridge Cambridgeshire CB3 9DQ UK Tel: 7913934052 [email protected]

Adolfo Botana

University of Toronto 1265 Military Trail Toronto, ON M1C 1A4 Canada [email protected]

Gregory Boutis

Brooklyn College/CUNY Department of Physics 2900 Bedford Avenue Brooklyn, NY 11210 Tel: 718 951 5000 x2873 [email protected]

Sean Bowen

Technical University of Denmark Ørsteds Plads Bygning 349, Rum 113 Kgs. Lyngby, 2800 Denmark Tel: +45 45253669 [email protected]

Joel Bradley

Cambridge Isotope Labs, Inc. 50 Frontage Road Andover, MA 01810 Tel: 978 749 8000 [email protected]

Scott Bradley

Eli Lilly and Company Lilly Corporate Center Indianapolis, IN 46285 Tel: 317-651-9685 [email protected]

John Breslin Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CA 95051 Tel: 650 424 4962 [email protected]

William W. Brey

National High Magnetic Field Lab / FSU 1800 E. Paul Dirac Drive Tallahassee, FL 32310 Tel: 850 645 3293 [email protected]

Douglas E. Brown

Indiana University 800 E. Kirkwood Ave., C237 Bloomington, IN 47405 Tel: 812-856-4629 [email protected]

Truman R. Brown

Medical Univ of SC 96 Jonathan Lucas Rd Charleston, SC 29564 Tel: 212 305-1864 [email protected]

Rafael Bruschweiler

Florida State University & NHMFL Department of Chemistry and Biochemistry 95 Chieftan Way Tallahassee, FL 32306 [email protected]

Evgeny Burmistrov

Los Alamos Nat Lab P. O. Box 1663, MS D454 Los Alamos, NM 87545 Tel: 1-505-665-6218 [email protected]

Timothy E Burrow

University of Toronto 80 St George Street Department of Chemistry Toronto, ON M5S 3H6 Canada Tel: 416-978-5728 [email protected]

Alex Burum

University of Miami 1103 Lisbon Coral Gables, FL 33134 [email protected]

Andrew Butler

Pfizer Worldwide R&D Eastern Point Road GROTON, CT 06340 Tel: (860) 715-4801 [email protected]

Olivier Buu


Luis Fernando Cabeça EMBRAPA Instrumentation 1452 XV de Novembro Street Sao Carlos, Sao Paulo 13560-970 Brazil Tel: 55 16 2107 2800 [email protected]

Sarah D. Cady

Iowa State University Chemical Instrumentation Facility 1234 Hach Hall Ames, IA 50011 Tel: 515-294-3941 [email protected]

Stefano Caldarelli

Aix Marseille University Campus Saint Jerome - Service 512 Marseille, bouche du rhone 13013 France [email protected]

Teresa Carlomagno

EMBL Meyerhofstrasse 1 Heidelberg, 69117 Germany Tel: 49 6221 3878552 [email protected]

Diego Carnevale

EPFL EPFL, ISIC, BCH Lausanne, Vaud 1015 Switzerland [email protected]

Maria Gabriela Aparecida Carosio

Institute of Chemistry of Sao Carlos 400 Trabalhador Sao-Carlense St, CP 780 Sao Carlos, Sao Paulo 13560-970 Brazil Tel: 55 16 3373 9946 [email protected]

Leah Casabianca

Weizmann Institute of Science 234 Hertzl Street Rehovot, Center 76100 Israel [email protected]

Fabio Casagrande

F. Hoffmann-La Roche AG Grenzacherstrasse 124 Basel, Baselstadt 4056 Switzerland Tel: +41 061 6880752 [email protected]

Julia Cassani

Uiversidad Autonoma Metropolit Calzada del Hueso 1100 Villa Quietud D.F, 4960 Mexico Tel: 54837255 [email protected]

John Cavanagh

North Carolina State University Biochemistry Department Campus Box 7622 126 Polk Hall Raleigh, NC 27695-7622 Tel: 919-513-4349 [email protected]


Page 124

Chaitanya Chandrana Los Alamos National Laboratory Los Alamos, NM 87544 [email protected]

S. Chandrashekar

New York University Dept. of Chemistry 100 Washington Square E. New York, NY 10003 Tel: 212 998 8450 [email protected]

Fa-An Chao

University of Minnesota 5-256 Hasselmo Hall 312 Church St SE Minneapolis, MN 55455 Tel: 612-626-2089 [email protected]

Ana Karina Chattah

FaMAF Facultad de Matematica Astronomia y Fisica Ciudad Universitaria Cordoba, South America X5016LAE Argentina Tel: +54(351)4334051 int 369 [email protected]

Mark Chaykovsky

Bruker BioSpin Corp. 15 Fortune Dr. Billerica, MA 01821 Tel: 978.667.9580 [email protected]

Eduard Chekmenev

Vanderbilt Univ Inst of Imaging Science 1161 21st Avenue South, AA3117 Nashville, TN 37232 Tel: 615-322-1329 [email protected]

Banghao Chen

Florida State University Chemistry and Biochemistry Dept Tallahassee, FL 32306 Tel: 850-644-3334 [email protected]

Kang Chen

National Institutes of Health Rm 3507, Bldg 50 50 South Drive Bethesda, MD 20892 Tel: 3015940451 [email protected]

Wen Chen

Rensselaer Polytechnic Institute 110 8th Street Biotech Center, Room 2232 Troy, NY 12180 Tel: 518-8606219 [email protected]

Kun Cheng Energy Biosciences Institute Calvin Lab 330 University of California, Berkeley Berkeley, CA 94720 Tel: 315-575-9353 [email protected]

Brian Cherry

Arizona State University 530 E. Orange St. Tempe, AZ 85287 Tel: 480-965-3613 [email protected]

Lingyu Chi

Missouri Univ of Science and Technology 400 W 11th Street, Rolla, MO 65409-0010 Rolla, MO 65401 Tel: 5736129421 [email protected]

Sandra Chimon Peszek

DePaul University 1110 W Belden Ave Chicago, IL 60614 Tel: 773-325-7473 [email protected]

Brad Chmelka

UCSB Department of Chemical Engineering Santa Barbara, CA 93106 Tel: 1-805-893-3673 [email protected]

James Chou

Harvard Medical School Biological Chemistry & Molecular Pharmacology 250 Longwood Ave., SGM 109 Boston, MA 02115 [email protected]

Martin Christen

University of Pittsburgh 3501 5th Avenue Dept. of Structural Biology Pittsburgh, PA 15260 Tel: 4123836939 [email protected]

Luisa Ciobanu

CEA/DSV/I2BM/Neurospin Bat 145, Point Courrier 156 Paris, Gif/Yvette F-91191 France [email protected]

Mary Clay

University of Illinois 601 S. Mathes Ave , 122A CLSL, Box 61-56, MC 712 Urbana, IL 61801 Tel: 2172441583 [email protected]

Marius Clore NIDDK, NIH Bldg 5, Rm B-30I Laboratory of Chemical Physics, Bethesda, MD 20892-0520 Tel: 3014960782 [email protected]

Laurie Close

Triangle Analytical 101 Pheasant Wood Ct Morrisville, NC 27560 Tel: 919 461 2300 [email protected]

Carlos Cobas

Mestrelab Research Felicano Barrera Fernandez 9B-BAIXO Santiago de Compostela, A Coruna 15706 Spain Tel: 34881976775 [email protected]

Ann Cochran

MR Resources 160 Authority Drive Fitchburg, MA 01420 [email protected]

Helga J Cohen

University of South Carolina Dept of Chemistry and Biochemistry 631 Sumter St Columbia, SC 29208 Tel: 803-777-2649 [email protected]

Jonathan Cole

Magnet Consultant Cryogenic Ltd Unit 30 Acton Park Estate, The Vale London, W3 7QE UK Tel: +44 (0) 208 743 6049 [email protected]

Kimberly L. Colson

Bruker BioSpin Corp. 15 Fortune Drive Billerica, MA 01821 Tel: 978-667-9580 x5114 [email protected]

Maria Concistre

University of Southampton School of Chemistry University Road Southampton, Hampshire SO171BJ UK Tel: 4.4023805941e+012 [email protected]

Chris Connors

Rensselaer Polytechnic Institute 110 8th St. Biotech 2232 Troy, NY 12180 [email protected]


Page 125

Paul Coote Harvard School of Engineering and Applied Sciences 33 Oxford Street, MD340 Cambridge, MA 02138 Tel: 6172336528 [email protected]

Marcy C Corey

JEOL USA, INC 11 Dearborn Road Peabody, MA 01960 Tel: 978-535-5900 [email protected]

Claudia C. Cornilescu

University of Wisconsin-Madison 433 Babcock Dr Biochemistry Bldg Room B160C Madison, WI 53706 Tel: 608-261-1166 [email protected]

Gabriel Cornilescu

University of Wisconsin - Madison 433 Babcock Drive, Rm. B160F Biochemistry Department Madison, WI 53706-1544 Tel: (608)-261-1166 [email protected]

Bob Corte

Bruker Impact Unlimited 250 Ridge Road Dayton, NJ 8810 Tel: 732.274.2000 [email protected]

Denis Courtier-Murias

Univ. of Toronto Dept of Chemistry, 1265 Military Trail Toronto, ON M1C 1A4 Canada [email protected]

Bruce Coxon

National Institutes of Health 31 Center Drive, Room 2A25 MSC 2423 Bethesda, MD 20892 Tel: 301-295-4780 [email protected]

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ReMarcus Curry

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Eugenio Daviso

Brandeis University Dept. of Chemistry Waltham, MA 02454-9110 Tel: 6178201811 [email protected]

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University of Florida 214 Leigh Hall Gainesville, FL 32611 Tel: 3528704912 [email protected]

Nicola De Zanche

University of Alberta Medical Physics / Oncology 11560 University Avenue Edmonton, AB T6G 1Z2 Canada Tel: 780-989-8155 [email protected]

Frank Decker

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Gregory DeKoster Washington University School of Medicine 660 S. Euclid Ave. St. Louis, MO 63110 Tel: 314-362-8885 [email protected]

Frank Delaglio


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Wuhan Institute of Physics and Mathematics, Chines West No.30 Xiao Hong Shan, Wuchang, Wuhan, China Wuhan, 430071 China Tel: 8.6027871988e+012 [email protected]

Dan Dennehy

Cambridge Isotope Lab 50 Frontage Rd Andover, MA 01810 Tel: 978 749 8000 [email protected]

Philip R Dennison

UC Irvine 1102 Natural Sciences II Dept of Chemistry, UC Irvine Irvine, CA 92697 Tel: 949 824 6010 [email protected]

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Michael Deschamps Universite d'Orleans CNRS-CEMHTI 1D, Avenue de la Recherche Scientifique Orleans, Centre 45000 France Tel: +33 2 38 25 55 11 [email protected]

Stephen DeVience

Harvard University Department of Chemistry and Che 12 Oxford Street Cambridge, MA 02138 [email protected]

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Isotec 3858 Benner Road Miamisburg, OH 45342 [email protected]

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Rana Dorsey

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Merck 126 E. Lincoln Ave RY80L-101 Rahway, NJ 7065 Tel: 732-594-7089 [email protected]

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Doty Scientific 700 Clemson Road Doty Scientific Inc. Columbia, SC 29229 Tel: 803-788-6497 [email protected]

Glenn Doty

Doty Scientific, Inc. 700 Clemson Road Columbia, SC 29229 Tel: 803 788 6497 [email protected]

Judy Doty


Justin Douglas

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Helmut Duddeck

Leibniz Univ. Institute of Organic Chemistry Schneiderberg 1B Hannover, D-30167 Germany [email protected]

Dmytro Dudenko

Max-Planck-Inst for Polymer Research Ackermannweg 10 Mainz, Rheinland-Pfalz 55128 Germany Tel: -61753051 [email protected]

Venkat R. Dudipala University of Akron Dept of Chemistry 190E Buchtel Commons Akron, OH 44325 Tel: 330-972-8645 [email protected]

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Cambridge Isotope Labs, Inc. 50 Frontage Road Andover, MA 01810 Tel: 978 749 8000 [email protected]

Sneha Dugar

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Merck 2015 Galloping Hill Rd Kenilworth, NJ 7033 Tel: 908-740-4016 [email protected]

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Page 127

E. Vindana Ekanayake The Florida State University 3711 Shamrock St. W G236 Tallahassee, FL 32309 Tel: 850-298-8581 [email protected]

Uzi Eliav

School of Chemistry, Tel Aviv University Tel Aviv University, Ramat Aviv Tel Aviv, Middle east 69978 Israel Tel: 972 3 6407002 [email protected]

Paul Ellis

Doty Scientific 700 Clemson Road Columbia, SC 29229 Tel: 803 788 6497 [email protected]

Don Emerson

Resonance Consulting 10321 Ridgeline Drive Milan, MI 48160 Tel: 734 417 0577 [email protected]

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Tecmag 10161 Harwin, #150 Houston, TX 77479 Tel: 713 667 8747 [email protected]

Lyndon Emsley

ENS Lyon 46 Allee d'Italie Ecole Normale Superieure de Lyon Lyon, Lyon 69364 France Tel: 33 472728486 [email protected]

Yuki Endo

JEOL RESONANCE Inc. Musashino 3-1-2, Akishima Tokyo, 196-8558 Japan [email protected]

Frank Engelke

Bruker Biospin Silberstreifen 4 Rheinstetten, DE-76287 Germany Tel: +49 721 5161-129 [email protected]

Raul G. Enríquez

Instituto de Quimica, UNAM Ciudad Universitaria Mexico, Mexico City 4510 Mexico Tel: 52 55 55440004 [email protected]

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Richard R. Ernst Lab.f.Phys.Chemie, ETH Zürich Wolfgang Pauli Strasse 10 8093 Zürich, Switzerland [email protected]

Cristian Escobar FSU 187 Crenshaw Ct Apt 1 Tallahassee, FL 32310 Tel: 850 524 4832 [email protected]

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Ramrod Scientific, Inc. 10 Waterford Street PO Box 1163 Gardner, MA 01440 Tel: 978-632-5890 [email protected]

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University of South Carolina Swearingen Engineering Center Computer Science and Engineering Columbia, SC 29201 Tel: 8649089123 [email protected]

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University of Florida PO BOX 117200` Gainesville, FL 32611 Tel: 3523922345 [email protected]

Jarrett Farias

Agilent Technologies, Inc. 5301 Stevens Creek Blvd Mail Stop 2U - ZA Santa Clara, CA 95051 [email protected]

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Cambridge Univ Cambridge, UK [email protected]

Hashim Farooq

University of Toronto 1265 Military Trail Toronto, ON M1C 1A4 Canada Tel: 4162877251 [email protected]

Ju Feng

PNNL 2500 GWW, Apt. 126 Richland, WA 99354 Tel: 5093717147 [email protected]

Yesu Feng

Duke University FFSC 2305 124 Science Dr Durham, NC 27708-0354 Tel: 919-660-1587 [email protected]

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McMaster University 1280 Main St. W. Hamilton, ON L8S 4K1 Canada Tel: 905 525 9140 ext. 24194 [email protected]

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Military Institte of Engineering Parca General Tiburcio 80, Urca Rua Lauro Muller 16, apto, 402 Rio de Janeiro, South America 22290-270 Brazil Tel: (5521) 2546-7057 [email protected]

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Norell, Inc. PO Box 307 Landisville, NJ 8326 Tel: 609-909-3700 [email protected]

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PPG 440 College Park Drive Allison Park, PA 15101 Tel: 412-492-5187 [email protected]

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University of Virginia 409 Mccormick Rd Chemistry Building Charlottesville, VA 22904 Tel: 4349241429 [email protected]

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Open Technologies, Inc. 51639 Bluffside Ct Granger, IN 46530 Tel: 269-288-0273 [email protected]

Thomas Frederick

University of Notre Dame 251 Nieuwland Science Hall Notre Dame, IN 46556-5670 [email protected]

Jonas Fredriksson

Centro Nacional de Ressonancia Magnetica Nuclear, Avenida Carlos Chagas Filho 373 Ilha do Fundao Rio De Janeiro, RJ 21941902 Brazil [email protected]

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CBER/FDA 29 Lincoln Drive Building 29, Room 115, HFM-428 Bethesda, MD 20892 Tel: 301 496 0837 [email protected]


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Heather Frericks Schmidt Pfizer Inc 445 Eastern Point Road, 2037 Groton, CT 06340 Tel: 860-868-3156 [email protected]

Amy S Freund

Bruker Biospin 15 Fortune Dr. Billerica, MA 01821 Tel: (978) 667-9580 [email protected]

Michael Frey


Charles Fry

Univ of Wisconsin-Madison 1101 University Ave Chemistry Department Madison, WI 53706 Tel: 608 262 3182 [email protected]

Lucio Frydman

Weizmann Institute Chemical Physics Dept 200 Herzl St Rehovot, Rehovot 76100 Israel Tel: 972 8 934 4903 [email protected]

Biao Fu

Department of Chemistry University of Cambridge F3, Wolfson court, Clarkson Road Cambridge, Cambridgeshire CB30HD UK [email protected]

Josepha Fu

Nalco Company 1601 W. Diehl Road Naperville, IL 60563-1198 Tel: (630) 305-2347 [email protected]

Riqiang Fu

National High Magnetic Field Laboratory 1800 E Paul Dirac Drive Tallahassee, FL 32310 Tel: 8506445044 [email protected]

Naoyuki Fujii

JEOL UK ltd. JEOL House Silver Court Watchmead Welwyn Garden City Herts, AL7 1LT UK Tel: +44-(0)7977-469177 [email protected]

Kazuo Furihata University of Tokyo 1-1-1 Yayoi Bunkyou-ku Tokyo, 113-8657 Japan Tel: -11223 [email protected]

George Furst

University of Pennsylvania 250 S. 33rd St Philadelphia, PA 19104 Tel: 215-8983407 [email protected]

Michael M. Fuson

Denison University Dept of Chemistry and Biochemistry Granville, OH 43023 Tel: (740) 587-6782 [email protected]

José Félix Gómez Reyes

Departamento de Quimica, Centro de Investigacion y Av. IPN # 2508 Col. Zacatenco Mexico D.F., Mexico D.F. 7360 Mexico Tel: +(52-55)57473727 [email protected]

Gigi Galiana

Yale University 300 Cedar Street, N125 New Haven, CT 06511 Tel: 203-393-6779 [email protected]

Zhehong Gan

NHMFL 1800E Paul Dirac Drive Tallahassee, FL 32310 Tel: 850 644 4662 [email protected]

Paul Ganssle

UC Berkeley 208C Stanley Hall Berkeley, CA 94720 Tel: 510-642-2094 [email protected]

Xinfeng Gao

Indiana University 800 E. Kirkwood Ave. Bloomington, IN 47405 [email protected]

Piotr Garbacz

University of Warsaw Krakowskie Przemiescie 26/28 Warsaw, 00-927 Poland Tel: 48503131614 [email protected]

Erwin Garcia

LipoScience Inc. 2500 Sumner Blvd Raleigh, NC 27616 Tel: 716-908-8567 [email protected]

David Gardner MR Resources 160 Authority Drive Fitchburg, MA 01420 [email protected]

Michael Garwood

University of Minnesota CMRR 2021 6th Street S.E. Minneapolis, MN 55455 Tel: 612 626 7736 [email protected]

Julia Gath

ETH Zuerich Laboratorium fuer physikalische Chemie Wolfgang-Pauli-Str 10 Zuerich, 8093 Switzerland Tel: 0041-44 633 [email protected]

Cristina Geada

Mestrelab Research Feliciano Barrera Fernandez 9B-BAIXO Santiago de Compostela, Coruna 15706 Spain Tel: 34 881 976 775 [email protected]

Max Gemeinhardt

Southern Illinois University of Carbondale 1245 Lincoln Drive Neckers 102 Carbondale, IL 62901 Tel: 8153544748 [email protected]

Peter Genovese

JEOL 11 Dearborn Road Peabody, MA 01960 [email protected]

Rex Gerald

Missouri Univ of Science and Technology Department of Chemistry 306 Schrenk Hall Rolla, MO 65409 [email protected]

Bernd Gewiese

Bruker BioSpin GmbH Silberstreifen 4 Rheinstetten, Baden-Wurttemberg DE-76287 Germany Tel: +49 721 5161 6106 [email protected]

Ion Ghiviriga

University of Florida Chemistry Department, 108A CLB Gainesville, FL 32611-7200 Tel: 352-846-3001 [email protected]


Page 129

Eric Giacomini CEA Commisariat a L'energie Atomique Batiment 145 Neurospin Point Courrier 156 gif sur yvette, ile de france 91190 France Tel: 33169087489 [email protected]

Roberto R. Gil

Carnegie Mellon University 4400 Fifth Ave Pittsburgh, PA 15213 Tel: 412-268-4313 [email protected]

Barjor Gimi

Dartmouth Medical School 354W Borwell, One Medical Center Drive Biomedical NMR Research Ctr Lebanon, NH 3756 Tel: 603 650 3925 [email protected]

Patrick Giraudeau

Universite de Nantes CEISAM, Faculte des Sciences et Techniques BP 92208, 2 rue de la Houssiniere Nantes Cedex 03, Pays de la Loire France France Tel: 33251125709 [email protected]

John Glushka

University of Georgia 315 Riverbend Rd. Athens, GA 30602 Tel: 706-542-4483 [email protected]

Klaes Golman

Marsvej 4 Kregme, DK 3300 Denmark Tel: 4545570857 [email protected]

Sergey Golotvin

ACD/ Labs 8 King Street East, Suite 107 Toronto, ON M5C 1B5 Canada Tel: 416 368 3435 [email protected]

Jeremy Good

Managing Director Cryogenic Ltd Unit 30 Acton Park Estate, The Vale London, W3 7QE UK Tel: + (0)208 743 6049 [email protected]

Boyd M. Goodson

Southern Illinois University Dept of Chemistry and Biochemistry 113 Neckers Hall Carbondale, IL 62901 Tel: 618-453-6427 [email protected]

Vitaliy Gorbatyuk University of Conn./BBC 91 N. Ealgeville Rd. Unit-3149 Storrs, CT 06269-3149 Tel: (860) 486-5011 [email protected]

Federico Gottardo

University of Michigan 533A Longshore Drive Ann Arbor, MI 48105 Tel: 734-276-8864 [email protected]

Nagana Gowda

University of Washington Mitochondria and Metabolism Center, Anesthesiology and Pain Medicine UW Medicine and South Lake Union Seattle, WA 98195 Tel: 7655433018 [email protected]

Hanna Gracz

NMR Facility, NCSU 128 Polk Hall M & S Biochemistry Raleigh, NC 27695 Tel: 919 515 8907 [email protected]

Philip J. Grandinetti

The Ohio State University 100 West 18th Avenue Columbus, OH 43210 Tel: 614-292-6818 [email protected]

Christopher V. Grant

University of California San Diego Bubble Building, Parking lot 207 9500 Gilman Dr. 0127 La Jolla, CA 92093-0127 Tel: 858 8225931 [email protected]

Andrée Gravel

Universite du Quebec a Montreal 2101 rue Jeanne-Mance Montreal, QC H2X 1X7 Canada Tel: 514-987-3000 ext 4391 [email protected]

Andreas Greiner

University of Freiburg Dept of Microsystems Engineering Georges-Koehler-Allee 103 Freiburg, 79110 Germany Tel: 4.9761203738e+011 [email protected]

James Griffin

Florida State University 95 Chieftan Way Tallahassee, FL 32306 Tel: 412-477-2303 [email protected]

Robert Griffin MIT Dept. of Chemistry/FBML NW14-3220, 77 Mass Avenue Cambridge, MA 02139 Tel: 617 253-5597 [email protected]

Angela Gronenborn

University of Pittsburgh 3501 Fifth Avenue, 1051 BST3 Dept of Structural Biology Pittsburgh, PA 15260 Tel: 4126489959 [email protected]

Sandra Groscurth

Farberstrasse 35 Zurich, Zurich 8008 Switzerland [email protected]

Leonid Grunin

Mari State Technical University Lenin sq.3 Yoshkar-Ola, Mari El 424000 Russian Federation Tel: 79033261515 [email protected]

James Gruschus

Laboratory of Molecular Biophysics National Heart, Lung & Blood Institute National Institutes of Health Bethesda, MD 20892 Tel: 301-496-2350 [email protected]

Jun Gu

University of Pennsylvania Department of Chemistry University of Pennsylvani 231S. 34th Street Philadelphia, PA 19104-6323 Tel: 215-898-1302 [email protected]

Xudong Guan

University of Illinois 1206 W. Gregory Dr Urbana, IL 61801 Tel: 217 265 8019 [email protected]

Gerry Guilfoy

Cambridge Isotope Labs, Inc. 50 Frontage Road Andover, MA 01810 [email protected]

Sylvain Guimbaud

Bruker Physik GmbH Rudolf-Plankstr. 23 Ettlingen, Baden Wuertenberg 76275 Germany [email protected]

Brogan Gust

SIUC 1245 Lincoln Drive Room 102 Carbondale, IL 62901 Tel: 6184536266 [email protected]


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Martin Gustavsson University of Minnesota 6-155 Jackson Hall 321 Church St. SE Minneapolis, MN 55455 Tel: 612-625-0786 [email protected]

Rebecca Guza

H.B. Fuller 1200 Willow Lake Blvd Vadnais Heights, MN 55110 [email protected]

Eric Habib

McGill University 801 Sherbrooke West Montreal, QC H3A2K6 Canada Tel: 514-398-6229 [email protected]

El Mohamed Halidi

NanoNMRI UM2-CNRS L2C UMR5221 Place Eugene Bataillon, CC 026 Montpellier Cedex 5, Languedoc-Roussillon 34095 France Tel: 467143983 [email protected]

Mamoru Hamada

Japan Superconductor Technology, INC. 1-5-5 Takatsuka-dai, Nishi-ku Kobe, Hyogo 651-2271 Japan Tel: 81-78-991-9445 [email protected]

Shellie Hammond

MR Resources 160 Authority Drive Fitchburg, MA 01420 Tel: 978 345 9010 [email protected]

Fei Han

New York University Department of Chemistry New York, NY 10003 Tel: 2129988463 [email protected]

Kee Sung Han

Oak Ridge National Laboratory Chemical Sciencse Division Oak Ridge, TN 37831-6201 Tel: 865-576-2751 [email protected]

Oc Hee Han

Daegu Center Korea Basic Science Institute 1370 Sankyuckdong Bookgu Daegu, , 702-701 South Korea Tel: 82-53-950-7912 [email protected]

Songi Han

University of California Santa Barbara Department of Chemistry and Biochemistry 9510 Santa Barbara, CA 93106 Tel: 806 893 4858 [email protected]

Yun Han University of Delaware Dept of Chemistry and Biochemistry Newark, DE 19716 Tel: 3028318624 [email protected]

D. Flemming Hansen

ISMB, University College London Gower Street London, London WC1E 6BT UK Tel: +44 207 679 2238 [email protected]

Gerard Harbison

University of Nebraska-Lincoln 723 Hamilton Hall Lincoln, NE 68588-0304 Tel: 402-472-9346 [email protected]

Jason Harris

McGill University 801 Sherbrooke Street West Montreal, QC H3A 2K6 Canada Tel: 514-398-6230 [email protected]

Arnold Harrison

Rampant Technology Partners, LLC 1621 Janet Place South Charleston, WV 25303 Tel: 304 744 3831 [email protected]

Jerry Hatvany


Matt Hatvany

Triangle Analytical, Inc. 101 Pheasant Wood Court Morrisville, NC 27560 [email protected]

Erhard T.K. Haupt

Department Chemistry University Hamburg Martin-Luther-King-Pl. 6 Hamburg, Hamburg D-20146 Germany Tel: -45964 [email protected]

Kikuko Hayamizu

National Inst of Advanced Industrial Science AIST Tsukuba Center 2 Tsukuba, Ibaraki 305-8565 Japan Tel: -7104 [email protected]

Sophia E. Hayes

Washington University Department of Chemistry 1 Brookings Dr., Box 1134 Saint Louis, MO 63130 Tel: 314-935-4624 [email protected]

Steve Hayward ACD/Labs 8 King Street East, Suite 107 TORONTO, ON M5C 1B5 Canada [email protected]

Ping He

SIUC, department of Chemistry 224 Neckers Hall southern illinois university carbondale Carbondale, IL 62901 Tel: 618-453-6266 [email protected]

Qiuhong He

University of Pittsburgh B804-PUH, MRRC, UPMC 200 Lothrop Street Pittsburgh, PA 15213 Tel: 412-647-3088 [email protected]

John Heinrich

Revolution NMR LLC 4921 Eagle Lake Drive Fort Collins, CO 80524 Tel: 970 472 0613 [email protected]

Joseph A Helpern

Med Univ S. Carolina Dept of Radiology 96 Jonathan Lucas St, MSC 323 Charleston, SC 29425 Tel: 843-792-4637 [email protected]

Jeffery Hendrycks

ACD/Labs 8 King Street East, Suite 107 TORONTO, ON M5C 1B5 Canada [email protected]

Xiao Heng

UMBC 1000 Hilltop Circle Baltimore, MD 21250 [email protected]

Jürgen Hennig

University Hospital Freiburg Medical Physics, Department of Radiology Breisacher Straße 60a Freiburg, 79106 Germany [email protected]

Mirko Hennig

Medical University of South Carolina Dept. of Biochemistry and Molecular Biology PO Box 250509, 70 President St, DD213 Charleston, SC 29425 Tel: 843-876-2382 [email protected]

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Kurt Hermann W. L. Gore 4250 W. Kiltie Ln. Flagstaff, AZ 86001 Tel: 928-864-4354 [email protected]

Gonzalo Hernández

Vis Magnetica Americo Vespucio 1323/137 Montevideo, 11700 Uruguay Tel: 59899497254 [email protected]

Alvaro I Herrera

Kansas State University 141 Chalmers Hall Kansas State University Manhattan, KS 66506 Tel: 785-532-3108 [email protected]

Hermann Heumann

Silantes GmbH Gollierstr. 70c Munchen, 80339 Germany Tel: 011 49 89 500 941 18 [email protected]

Chandralal Hewage

University College Dublin Conway Institute Belfield Dublin 4, Dublin D4 Ireland Tel: 35317166870 [email protected]

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MRC Laboratory of Molecular Biology Hills Road Cambridge, CB2 0QH UK [email protected]

Christian Hilty

Texas A&M University 3255 TAMU College Station, TX 77845 [email protected]

Jeffrey C. Hoch

Univ of Connecticut Health Ctr Molecular, Microbial, and Structural Biology 263 Farmington Ave. Farmington, CT 06030-3305 Tel: 860-679-3566 [email protected]

Gregory P. Holland

Arizona State University Department of Chemistry and Biochemistry Arizona State University Tempe, AZ 85287-1604 [email protected]

Jim Hollenhorst Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CA 95051 Tel: 408 553-4327 [email protected]

Steven Hollis

Amgen Inc. 360 Binney St Cambridge, MA 02142 Tel: 617 444 5410 [email protected]

Laura Holte


Mei Hong

Iowa State Iowa State University Dept. Chem, Gilman Hall 0108 Ames, IA 50011 Tel: 515 294 3521 [email protected]

Jerris Hooker

National High Magnetic Field Laboratory 1800 E. Paul Dirac Dr Tallahassee, FL 32310 Tel: 8506444379 [email protected]

Cody Hoop

Univ of Pittsburgh 3501 Fifth Ave Structural Biology Pittsburgh, PA 15260 Tel: 7245548106 [email protected]

Joseph P. Hornak

RIT 54 Lomb Memorial Drive Center fo Imaging Science Rochester, NY 14623-5604 Tel: 585 475-2904 [email protected]

Ramakrishna V Hosur

Tata Institute of Fundamental Research Department of Chemical Sciences, Homi Bhabha Road, Mumbai, Maharashtra 400005 India Tel: 9.1222280455e+011 [email protected]

Guangjin Hou

University of Delaware 043 Brown Lab University of Delaware Newark, DE 19716 Tel: 302-831-8624 [email protected]

Yonatan Hovav Weizmann institute of science Herzel Rehovot, - 76100 Israel [email protected]

Peter Howe

Syngenta Jealott's Hill Research Centre Bracknell, Berkshire RG42 6EY UK Tel: 01344 424701 [email protected]

Jian Zhi Hu

Pacific Northwest National Laboratory 902 Battelle Blv, P.O. Box 999 MSIN K8-98 Richland, WA 99354 Tel: (509)371-6544 [email protected]

Jun Hu

AstraZeneca 35 Gatehouse Dr Waltham, MA 02451 [email protected]

Mary Hu

Pacific Northwest National Laboratory 3335 Q Ave Richland, WA 99354 Tel: 509-371-7529 [email protected]

Weiguo Hu

UMass Amherst Conte Research Center 120 Governor's Dr. Amherst, MA 01003 [email protected]

Danting Huang

Florida State University 2525 Pottsdamer Street, Building A, Suite A131 Tallahassee, FL 32310 Tel: 850-728-5092 [email protected]

Dee-Hua Huang

The Scripps Research Institute 10550 N. Torrey Pines Rd. La Jolla, CA 92037 Tel: (858) 784-2329 [email protected]

Shaw Huang

Harvard University Dept. of Chemistry & Chemical Biology 12 Oxford Street Cambridge, MA 02138 Tel: 6174953939 [email protected]

Xi Huang

Department of Chemistry, Univ of Florida PO Box 117200, Gainesville, Florida 32611 Gainesville, FL 32611 Tel: 3522226261 [email protected]


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Matthias Huber ETH Zurich Physical Chemistry Wolfgang Pauli Strasse 10 Zurich, ZH 8093 Switzerland Tel: -4983 [email protected]

Alan Hume

Bruker Ltd. 555 Steeles Ave. East Milton, ON L9T 1Y6 Canada [email protected]

Ivan Hung

National High Magnetic Field Laboratory 1800 E. Paul Dirac Drive Tallahassee, FL 32310 Tel: 850-645-8914 [email protected]

Ralph Hurd

GE Healthcare 333 Ravenswood Ave Menlo Park, CA 94025 Tel: 4083941820 [email protected]

Ryeo yun Hwang

Korea Basic Science Institute(Analysis Research Di 1370 Sankyuckdong, Bookgu Daegu, 702-701 South Korea Tel: 86-10-4641-9344 [email protected]

Tsang-Lin Hwang

AMGEN One Amgen Center Drive Thousand Oaks, CA 91320 Tel: (805) 447-4921 [email protected]

Sven G. Hyberts

Harvard Medical School Dept. BCMP 240 Longwood Ave. Boston, MA 02115 Tel: 617-432-1721 [email protected]

Tatyana Igumenova

Texas A&M University Dept of Biochemistry and Biophysics 300 Olsen Boulevard, TAMU 2128 College Station, TX 77843 Tel: 9798456312 [email protected]

Mitsu Ikura

Ontario Cancer Institute University Health Network 101 College Street, 4th floor room 804 Toronto, ON M5G 1L7 Canada Tel: 416-581-7550 [email protected]

Carson Ingo University of Illinois at Chicago 300 N State #5229 Chicago, IL 60654 [email protected]

Stephanie Irausquin

University of South Carolina 1200 Catawba Street Columbia, SC 29208 Tel: 8039609563 [email protected]

Yoshitaka Ishii

Univ. Illinois at Chicago 845 W Taylor St. Department of Chemistry Chicago, IL 60607 Tel: 312-413-0076 [email protected]

Rieko Ishima

University of Pittsburgh Rm 1037, BST3 3501 5th Avenue Pittsburgh, PA 15260 Tel: 412-648-0645 [email protected]

Shin Isogai

Biozentrum, Abteilung Strukturbiologie, Universita Klingelbergstrasse 70 Basel, 4056 Switzerland Tel: +41 61 267 2107 [email protected]

Arnold Itkin

NMR Associates 150 River Street Fitchburg, MA 01420 [email protected]

Christian Jaeger

BAM Federal Institute of Materials Research and Te Richard Willstaetter Str. 12 Berlin, Berlin D-12489 Germany Tel: +49 30 8104 1131 [email protected]

Lukasz Jaremko

University of Warsaw Krakowskie Przedmiescie 26/28 Warsaw, Mazovia 927 Poland Tel: 48694267950 [email protected]

Mariusz Jaremko

Institute of Biochemistry and Biophysics PAS Pawinskiego 5a Warsaw, Mazovia 2106 Poland Tel: 48696922325 [email protected]

Thusitha Jayasundera Boston College Merkert Chemistry Center 2609 Beacon Street Chestnut Hill, MA 02467 Tel: 617-552-6984 [email protected]

Frantz L. Jean-francois

NHMFL 2750 Old St. Augustine Rd. Apt. B-15 1800 East Paul Dirac Dr. Tallahassee, FL 32310 Tel: 850 728 0590 [email protected]

Stefan Jehle

Center for NMR At Very High Fields - CNRS Lyon 5, rue de la Doua Villeurbanne, Rhone-Alpes 69100 France Tel: +33 (0) 426233881 [email protected]

Kendra R Jendro

Bruker BioSpin Corporation 15 Fortune Drive Manning Park Billerica, MA 01821 Tel: 978-667-9580 ext. 5218 [email protected]

Elias J Jeyarajah

LipoScience, Inc 2500 Sumner Blvd Raleigh, NC 27616 Tel: 919 256 1131 [email protected]

Fangling Ji

University of Pittsburgh 1050 BST3, 3501 Fifth Ave. Pittsburgh, PA 15261 Tel: 4123308909 [email protected]

Karen Johnston

University of Windsor 143 McKay Avenue Apartment 1 Windsor, ON N9B 1Z3 Canada Tel: 5197909440 [email protected]

Chris Jones

Agilent Technologies 5301Stevens Creek Blvd Santa Clara, CA 95051 [email protected]

Louis Jones

University of California, Santa Barbara 817 De La Vina St Unit D Santa Barbara, CA 93101 [email protected]

Paul Jonsen

Revolution NMR 4921 Eagle Lake Drive Fort Collins, CO 80524 [email protected]


Page 133

Antoni Jurkiewicz University of Chicago Department of Chemistry 5735 S.Ellis Ave., Chicago, IL 60637 Tel: 7738347420 [email protected]

Pavel Kaderavek

Masaryk University Kamenice 5 Brno, CZ 62500 Czech Republic [email protected]

Kumar Kaluarachchi

MD Anderson Cancer Center 1901 East Road Houston, TX 77054 Tel: 713-792-3779 [email protected]

Paul Kanyha

Tecmag 10161 Harwin Drive, S-150 Houston, TX 77479 Tel: 713 667 8747 [email protected]

Jeff Kao

Washington University Dept. of Chemistry One Brookings Drive St. Louis, MO 63130 Tel: 314 935 6833 [email protected]

Rob Kaptein

Utrecht University Padualaan 8 Utrecht, 3584CH Netherlands Tel: 0031-345-548718 [email protected]

Roger Kautz

Barnett Institute of Chem and Biol Analysis Northeastern University 360 Huntington Ave. Room 341 Mugar Hall Boston, MA 02115 Tel: 617 373 8211 [email protected]

Eric Keeler

The Ohio State University 100 W. 18th Ave Columbus, OH 43210 Tel: (614) 292-8064 [email protected]

Paul Keifer

Agilent Technologies, Inc 5301 Stevens Creek Blvd. M/S 2U-ZA Santa Clara, CA 95051 Tel: 650-533-4398 [email protected]

Jim Kempf Rensselaer Polytechnic Inst. 110 8th Street 209a Cogswell Lab Troy, NY 12180 Tel: 518-276-3951 [email protected]

Arno P.M. Kentgens

IMM, Radboud University Heyendaalseweg 135 Nijmegen, 6525 AJ Netherlands [email protected]

Dorothee Kern

Brandeis University Boston, MA 0 [email protected]

Klemens Kessler

Bruker BioSpin AG Industriestrasse 26 Faellanden, 8117 Switzerland Tel: 0041 44 825 9698 [email protected]

John Key

Lakeshore Cryotronics 575 McCorkle Blvd Westerville, OH 43081 Tel: 614 212 1525 [email protected]

Philip Keyes

Lexicon Pharmaceuticals 350 Carter Road Princeton, NJ 8540 Tel: 609-466-5596 [email protected]

CL Khetrapal

Center of Biomedical Magnetic Resonance Sanjay Gandhi Postgraduate Institute of Medical Sciences Raebareli Road Lucknow, Uttar Pradesh 226014 India [email protected]

Gennady Khirich

Yale University 350 Edwards St. New Haven, CT 06511 Tel: 347-536-6049 [email protected]

Aleksandra Kijac

University of California San Francisco Institute for Neurodegenerative Diseases 513 Parnassus Ave, Room HSE-771 San Francisco, CA 94143 Tel: 217-766-5766 [email protected]

John Kilby

New Era Enterprises Po Box 747 Vineland, NJ 08362-0747 [email protected]

Jieun Kim University of Kansas Medical Center 3901 Rainbow Blvd, MS 1052 Kansas City, KS 66160 [email protected]

Seho Kim

Rutgers University Department of Chemistry 610 Taylor Road Piscataway, NJ 8854 Tel: 732-445-1288 [email protected]

Monica Kinde

1215 Arapahoe St. Apt. 206 Lincoln, NE 68502 Tel: 4028178870 [email protected]

Robert Kinsey

Goodyear Tire & Rubber Company 142 Goodyear Blvd Akron, OH 44305 Tel: 330-796-4324 [email protected]

Andrew Kiruluta

Harvard University 17 Oxford St Cambridge, MA 02138 Tel: 617-947 6425 [email protected]

Masashi Kitamura

National Defense Academy 1/10/2020 Yokosuka, Hashirimizu 239-8686 Japan [email protected]

Alex Kitaygorodskiy

Clemson University 475 Hunter Hall Chemistry Department Clemson, SC 29634-0973 Tel: 864 656 0611 [email protected]

Jason Kitchen

National High Magnetic Field Laboratory 1800 E. Paul Dirac Dr. Tallahassee, FL 32310 Tel: 8506444197 [email protected]

Douglas A Klewer

Huntsman 8600 Gosling Rd The Woodlands, TX 77381 Tel: (281) 719-7607 [email protected]

Takeshi Kobayashi

Ames Laboratory 229 Spedding Hall, Ames Laboratory Iowa State University Ames, IA 50011 Tel: (515)294-6823 [email protected]


Page 134

Jurgen Kolz ACT GmbH Pauwelsstr. 19 Aachen, 52074 Germany Tel: 49 241 963 1423 [email protected]

Richard Komoroski

University of Cincinnati Center for Imaging Research PO Box 670583 Cincinnati, OH 45267-0583 Tel: 513 558 2391 [email protected]

Fangming Kong

Pfizer 445 East Point Road Groton, CT 06340 Tel: 860-715-6823 [email protected]

Xueqian Kong

UCB and LBNL C/O Reimer Lab 201 Gilman Hall UC Berkeley Berkeley, CA 94720 Tel: 5106433073 [email protected]

Janusz Koscielniak

NCI-Frederick, Inc. PO Box B Frederick, MD 21702 Tel: 301-846-5213 [email protected]

Anna Kozlova

FSU Institute of Molecular Biophysics Kasha Laboratory, MC4380 Tallahassee, FL 32306 Tel: 253-222-8564 [email protected]

Holger Kracke

University of Mainz Staudingerweg 7 Mainze, D-55128 Germany [email protected]

Krish Krishnamurthy


Damodaran Krishnan Achary

University of Pittsburgh 219 Parkman Avenue Pittsburgh, PA 15260 Tel: 4125086959 [email protected]

Ashok Krishnaswami


Leonid Krivdin Editor, Magnetic Resonance in Chemistry 1 Favorsky St. Irkutsk, 664033 Russian Federation Tel: +7(914)8974133 [email protected]

Robert Krull

Bruker BioSpin Corp. 15 Fortune Dr. Billerica, MA 01821 Tel: 978-667-9580 x5457 [email protected]

Bashar Ksebati

Wayne State University 410 W. Warren Ave. Detroit, MI 48202 Tel: 313 577 3100 [email protected]

Till Kuehn

Bruker BioSpin AG Industriestrasse 26 Faellanden, Zuerich 8117 Switzerland Tel: 0041 44 825 9538 [email protected]

Rainer Kuemmerle

Bruker Industriestrasse 26 Fallanden, 8117 Switzerland Tel: 41 44 825 9535 [email protected]

Rohtash Kumar

Isotec 3858 Benner Road Miamisburg, OH 45342 Tel: 937 859 1808 [email protected]

Eriks Kupce

Agilent Technologies 6, Mead Road Yarnton Oxford, Oxfordshire OX5 1QU UK [email protected]

Nicholas Kuzma

University of Pennsylvania 3450 Hamilton Walk Stemmler Hall Room 308 Philadelphia, PA 19104-6142 Tel: 215-746-4676 [email protected]

Anna Kuznetsova

Depts of Chemistry & Biochemistry McKnight Brain Inst, University of Florida 100 S. Newell Drive Bldg. 59, LG-129 Gainesville, FL 32611 Tel: 3522940140 [email protected]

Vladimir Ladizhansky

University of Guelph 50 Stone Rd. E. Department of Physics Guelph, ON N1G 2W1 Canada Tel: 519-8244120 ext. 53989 [email protected]

Timothy Laker Isotec 3858 Benner Road Miamisburg, OH 45342 Tel: 937 859 1808 [email protected]

Derek Langeslay

University of California, Riverside 180 W Big Springs rd #19 riverside, CA 92507 Tel: 6518082360 [email protected]

Steven LaPlante

Boehringer Ingelheim (Canad) Ltd. 2100 Cunard St. Laval, QC H7H2G9 Canada Tel: 450-682-4640 [email protected]

Sacha Larda

University of Toronto 3359 Mississauga Rd. N Mississauga, ON L5L1C6 Canada Tel: 4168982395 [email protected]

Frank Laukien

Bruker BioSpin 15 Fortune Drive Billerica, MA 01821 Tel: 978 667 9580 [email protected]

Regan LeBlanc

University of Maryland, College Park 1441 Rhode Island Ave NW Apt 119 Washington, DC 20005 Tel: 2024946506 [email protected]

Jae-Seung Lee

New York University Department of Chemistry New York University New York, NY 10003 Tel: 212-998-8463 [email protected]

Jung Ho Lee

University of Wisconsin-Madison 1101 University Ave Madison, WI 53706 Tel: 608-695-5566 [email protected]

Donald Leek

National Research Council Canada 100 Sussex Drive Ottawa, ON K1A0R6 Canada Tel: 613-286-8071 [email protected]

Moreno Lelli

ENS Lyon/CNRS 5, Rue de la Doua Villeurbanne, Rhone-Alpes 69100 France Tel: 33786009618 [email protected]


Page 135

Pietro Lendi Bruker Industriestrasse 26 Faellanden, 8117 Switzerland [email protected]

Gregory Leo

Janssen Pharmaceutical Companies of J & J Welsh & McKean Roads Spring House, PA 19477-0776 Tel: 215-628-5884 [email protected]

Sarah Leonard

The Florida State University Dept of Chemical and Biomedical Engineering 2525 Pottsdamer St., A131 Tallahassee, FL 32310 Tel: 941-400-1613 [email protected]

Eric Leonardis

Bruker Biospin 34 rue de l'industrie Wissembourg, 67166 France Tel: 33688058178 [email protected]

Anne Lesage

University of Lyon, High Field NMR Center 5 rue de la DOUA Villeurbanne, France 69100 France Tel: 33 4 26 23 38 75 [email protected]

Patricia Levstein

FAMAF Universidad Nacional de Cordoba Cordoba, CP:X5000HUA Argentina [email protected]

David Lewis

Revolution NMR LLC 4921 Eagle Lake Dr., Unit C Fort Collins, CO 80524 Tel: 970 493 6600 [email protected]

Hongde Li

Wuhan Institute of Physics and Mathematics, the Ch West No.30 Xiao Hong Shan wuhan, Hubei province 430071 China Tel: 8.6158270482e+012 [email protected]

Jing Li

International Flavors and Fragrances 1515 Highway 36 Union Beach, NJ 7735 Tel: 1-540-808-3526 [email protected]

Yang Li

University of Wyoming 267 N. 8th street, apartment 9 Laramie, WY 82072 Tel: 307-399-3885 [email protected]

Yi-Xin Li Bristol-Myers Squibb Co. 311 Pennington Rocky-Hill Rd. Bldg 13, rm 011 Pennington, NJ 8534 Tel: 1-609-818-6272 [email protected]

Zhao Li

UCLA Dept of Chemistry and Biochemistry 607 Charles E. Young Drive East Los Angeles, CA 90095-1569 Tel: 310-825-0491 [email protected]

Timo Liimatainen

University of Eastern Finland A.I.Virtanen Institute P.O.Box 1627 Kuopio, Europe 70211 Finland Tel: +358 40 355 3903 [email protected]

Allison Lin

Shigemi, Inc. 4790 Route 8, #21 Allison Park, PA 15101 Tel: 724 444 3011 [email protected]

Mike Lin

Shigemi, Inc. 4790 Route 8, #21 Allison Park, PA 15101 Tel: 724 444 3011 [email protected]

Ping-Chang Lin

University of Kansas Medical Center 3901 Rainbow BLVD Kansas City, KS 66160 [email protected]

Yung-Ya Lin

Department of Chemistry & Biochemistry, UCLA 607 Charles E. Young Dr. East Department of Chemistry & Biochemistry Los Angeles, CA 90095-1569 Tel: (310) 206-9887 [email protected]

Kresten Lindorff-Larsen

Department of Biology, University of Copenhagen Copenhagen Biocenter Ole MaalÃ¸es Vej 5 Copenhagen, DK-2200 Denmark Tel: +45 3532 2027 [email protected]

Diana M Lindquist

Cincinnati Children's Hsp Med 3333 Burnet Ave, ML 5033 Cincinnati, OH 45229 Tel: 513-636-9268 [email protected]

Rasmus Linser BCMP, Harvard Medical School Department of Biol. Chem. and Molec. Pharm., C1 building 240 Longwood Ave. Cambridge, MA 02115 Tel: 4.9176966535e+012 [email protected]

Stephanie Lisco

Isotec 3858 Benner Road Miamisburg, OH 45342 Tel: 937-859-1808 [email protected]

Maili Liu

Wuhan Institute of Physics and Mathematics, Chines West No.30 Xiao Hong Shan, Wuchang, Wuhan, China Wuhan, 430071 China [email protected]

Joanna R. Long

University of Florida Box 100245 Gainesville, FL 32610-0245 Tel: (352)846-1506 [email protected]

Liam Longo

Florida State University 1115 West Call Street Tallahassee, FL 32306-4300 Tel: 772 361 9697 [email protected]

James Longstaffe

Department of Chemistry University of Toronto 1265 Military Trail Toronto, ON M1C 1A4 Canada [email protected]

Christopher Lopez

3340 sw 23 st miami, FL 33145 Tel: 804-972-2875 [email protected]

J. Patrick Loria

Yale University Dept. of Chemistry P.O. Box 208107 New Haven, CT 06520 Tel: 203 436-4847 [email protected]

Judit Losonczi


Thomas J Lowery

T2 Biosystems 101 Hartwell Avenue Lexington, MA 02421 Tel: 781-457-1223 [email protected]


Page 136

Jiaozhi LU University of California at San Diego 9500 Gilman Drive San Diego, CA 92037 [email protected]

Sorin Luca

University of Nebraska Medical Center 986025 Nebraska Medical Center COP 3034 Omaha, NE 68198-6025 Tel: 402-559-1084 [email protected]

Sarah Luchsinger

Bruker BioSpin 15 Fortune Drive Billerica, MA 01281 Tel: 978-667-9580x5267 [email protected]

Bryan Lucier

University of Windsor 401 Sunset Ave Windsor, ON N9B3P4 Canada Tel: 519-253-3000 x4241 [email protected]

Bryan Lucier

University of Windsor 401 Sunset Ave Windsor, ON N9B3P4 Canada Tel: 519-253-3000 x4241 [email protected]

Lloyd Lumata

University of Texas Southwestern Medical Center 2201 Inwood Rd NE4.308 Dallas, TX 75390-8568 Tel: 214-645-2259 [email protected]

Werner E. Maas

Bruker Biospin 15 Fortune Drive Billerica, MA 01821 Tel: 978 667 9580 [email protected]

Luciana Elena Machado

Federal University of Rio de Janeiro Carlos Chagas Filho, 373, Bloco K, anexo CNRMN, Cidade Universitaria 263 Farmington Avenue, Farmington, Connecticut, 06030-3305 Rio de Janeiro 21941-590 Brazil Tel: (21)31042326 [email protected]

Slobodan Macura

Mayo Foundation 200 First Street SW Stabile SL-035 Rochester, MN 55905 Tel: 507 2845917 [email protected]

Louis A Madsen Virginia Tech Dept of Chemistry (0212) Blacksburg, VA 24061 Tel: 540-231-1270 [email protected]

Luís Mafra

University of Aveiro Departamento de Quimica 3810-193 Aveiro Aveiro, 351 Portugal Tel: 00351 927994275 [email protected]

Alviclér Magalhães

IQ UNICAMP Rua Monteiro Lobato s/n Campinas, Sao Paulo 13083-970 Brazil Tel: +55 19 35218794 [email protected]

Richard L. Magin

Univ. of Illinois at Chicago UIC, Dept. of BioE, MC 063 851 South Morgan St. Chicago, IL 60607 Tel: 312-996-2335 [email protected]

Melody Mak-Jurkauskas

Amgen 360 Binney St Cambridge, MA 02142 Tel: 6174445276 [email protected]

Sergey Maltsev

Miami University, OH 517 Wells Mill Dr Oxford, OH 45056 [email protected]

Thorsten Maly

Bridge12 Technologies, Inc. 37 Loring Drive Framingham, MA 01702 Tel: +1 617 615 9332 [email protected]

Soumyajit Mandal

Schlumberger-Doll Research 1 Hampshire Street Cambridge, MA 02139 Tel: 1 617 7682139 [email protected]

Suraj Manrao

Isotec Stable Isotopes Post Box 588 Old Bridge, NJ 8857 Tel: 732-310-2677 [email protected]

Wenping Mao

National High Magnetic Field Laboratory 1800 E Paul Dirac Drive Tallahassee, FL 32310 [email protected]

Bill Marathias Agilent Technologies 66 Taylor Rd Boston, MA 0172- [email protected]

Carla Marchioro

Aptuit Research Ctr Via Fleming 4 Verona, Verona 37135 Italy Tel: 39 045 8218 362 [email protected]

Silvia Mari

S. Raffaele Scientific Institute via Olgettina 58 Milan, Milan 20132 Italy Tel: -26434311 [email protected]

Evgeny Markhasin

Massachusetts Institute of Technology 166 Albany St., NW14-5117 Cambridge, MA 02139 [email protected]

Vered Marks

University of Miami 4721 N 37 st Hollywood, FL 33021 Tel: 954 6659719 [email protected]

Rachel W. Martin

UC Irvine 4136 Natural Sciences 1 Dept. of Chemistry UC Irvine Irvine, CA 92697-2025 Tel: 949 302-6040 [email protected]

Charlotte Martineau

Institut Lavoisier de Versailles (ILV) ILV/UVSQ 45 Avenue des Etats-Unis Versailles, Ile de France 78035 France Tel: 33139254260 [email protected]

Hussain Masoom

University of Toronto 1265 Military Trail Scarborough, ON M1C 1A4 Canada [email protected]

Ann McDermott

Columbia University 3000 Broadway, MC 3113 New York, NY 10027 [email protected]

Dan McElheny

UIC 845 W. Taylor Chicago, IL 60607-7061 Tel: 312-413-0082 [email protected]


Page 137

David McGarvey U.S. Army 5183 Blackhawk Road E-3330 Room 75 Gunpowder, MD 21010 Tel: 4437943102 [email protected]

Steve McKenna

Ineos Technologies, M/S F-9 PO Box 3011 Naperville, IL 60563 Tel: 630-961-7846 [email protected]

Michael T. McMahon

Johns Hopkins University SOM/KKI F.M. Kirby Research Center, KKI 707 N. Broadway Ave. Baltimore, MD 21205 Tel: 410-502-8188 [email protected]

Michael Meadows

Auburn University 179 Chemistry Building Auburn, AL 36849 Tel: (334)844-6993 [email protected]

Doug Meinhart

Bruker BioSpin 15 Fortune Drive Billerica, MA 01821 Tel: 978-495-2414 [email protected]

Kevin Meldrum


Erick Alejandro Meneses Ramirez

McGill University Department of Chemistry 845 Sherbrooke St. W. Pulp and paper Building room 304 Montreal, QC H3A 2T5 Canada Tel: 5143986230 [email protected]

Sonia C Menezes

PETROBRAS/CENPES Av. Horacio Macedo, 950- Cidade Universitaria Rio de Janeiro, RJ 21941-598 Brazil Tel: + 55 21 21626171 [email protected]

Matthew E Merritt

UT Southwestern Medical Center 5323 Harry Hines Blvd, NE4.2 Dallas, TX 75390 Tel: (214) 645-2727 [email protected]

Kenneth Metz Boston College Chemistry Dept. 2609 Beacon Street Chestnut Hill, MA 02467 Tel: 617 552 6488 [email protected]

Yimin Miao

NHMFL 924 W Pensacola St Apt A2 Tallahassee, FL 32304 Tel: 8505663208 [email protected]

Shalom Michaeli

CMRR University of Minnesota 2021 6th St. SE Minneapolis, MN, MN 55455 Tel: 612 607 2888 [email protected]

Vladimir K. Michaelis

Francis Bitter Magnet Lab, MIT 150 Albany St. Cambridge, MA 02139 Tel: 857-600-6391 [email protected]

Carl A. Michal

University of British Columbia Department of Physics and Astronomy 6224 Agricultural Rd Vancouver, BC V6T 1Z1 Canada Tel: 604 822-2432 [email protected]

Pascal Mieville

Ecole Polytechnique Federale de Lausanne batochime Lausanne, VD 1015 Switzerland Tel: +4121 693 98 36 [email protected]

Bozhana Mikhova

Institute of Organic Chemistry, Bulgarian Academy Acad. G. Bonchev Str. Bl.9 1113 Sofia Hemus Str. 37 Bl. 24 Entr. 3 Sofia, Europe 1111 Bulgaria Tel: 3.5989890481e+011 [email protected]

Teresa Miletti

McGill University 801 Sherbrooke St. West Montreal, QC H3A 0B8 Canada Tel: 514-398-6230 [email protected]

Karla Miller

FMRIB Centre John Radcliffe Hospital Headington Oxford, OX3 9DU UK [email protected]

Kevin Millis Cambridge Isotope Labs, Inc. 50 Frontage Rd Andover, MA 01810 Tel: 978-749-8000 [email protected]

Jamie Mills

Isotec 3858 Benner Road Miamisburg, OH 45342 Tel: 937 859 1808 [email protected]

Mark Milton

Millennium: The Takeda Oncology Company 40 Landsdowne St Cambridge, MA 02139 Tel: 6175512940 [email protected]

Prasanna Mishra

Mayo Foundation 200 First Street SW Rochester, MN 55905-0001 Tel: 507-284-0191 [email protected]

Odingo Mitchell

Brooklyn College Physics Department 2900 Bedford Ave Brooklyn, NY 11210 Tel: 3472183257 [email protected]

Anthony K Mittermaier

McGill University 801 Sherbrooke St. W Chemistry Department Montreal, QC H3A 0B8 Canada Tel: 514-398-3085 [email protected]

Takuya Miyakawa

The University of Tokyo 1-1-1 Yayoi, Bunkyo-ku Tokyo, Asia 113-8657 Japan Tel: -10929 [email protected]

Veera Mohan Rao

Indian Institute of Chemical Technology Centre for NMR and Structural Chemistry Uppal Road, Tarnaka Hyderabad, Andhra Pradesh 500007 India Tel: +91 9912047046 [email protected]

Andrii Monastyrskyi

University of South Florida 30239 USF Holly Dr Tampa, FL 33620 Tel: 8133344197 [email protected]


Page 138

Tony D Montina University of Lethbridge Dept of Chemistry and Biochemistry 4401 University Drive West Lethbridge, AB T1K 3M4 Canada Tel: 1-403-394-3927 [email protected]

Chulsoon Moon

SK Innovaation Global Technology SK Innovation, 325, Exporo Yuseong-Gu Daejeon, 305-712 South Korea [email protected]

Victoria Mooney

Yale University 225 Prospect St. New Haven, CT 06520 [email protected]

Krystal A. Morales

Texas A&M University 130 Olsen Boulevard Room N120 College Station, TX 77843 Tel: (979)845-6313 [email protected]

Kelly Moran

Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CA 95051 Tel: 8479446085 [email protected]

Corey Morcombe


Steven Morgan

Brooklyn College 2900 Bedford Ave. Brooklyn, NY 11210 [email protected]

Martha Morton

University of Nebraska - Lincoln 834 Hamilton Hall Lincoln, NE 68588 Tel: 402-472-6255 [email protected]

Detlef Moskau

Bruker BioSpin AG Industriestrasse 26 Faellanden, Zurich 8117 Switzerland Tel: +41 44 825 91 11 [email protected]

Kaustubh Mote

Dept. of Chemistry University of Minnesota 5-256, Nils Hasselmo Hall 312, Church ST SE Minneapolis, MN 55455 Tel: 612-812-3638 [email protected]

Christina Mozes Medical Univ of S Carolina 70 President St Charleston, SC 29425 Tel: 843 876 2378 [email protected]

Geoffrey A. Mueller

NIEHS/NIH 111 T.W. Alexander Drive MD-MR01 Research Triangle Park, NC 27709 Tel: 919-541-3872 [email protected]

Karl Mueller

Pacific Northwest National Laboratory 902 Battelle Boulevard. MSIN K8-98 Richland, WA 99352 Tel: 509-371-6550 [email protected]

Leonard J Mueller

University of California, Riverside Department of Chemistry Riverside, CA 92521 Tel: 951-827-3565 [email protected]

Luciano Mueller

Bristol-Myers Squibb Route 206 & Provinceline Road P. O. Box 4000 Princeton, NJ 08543-4000 Tel: 609 2524360 [email protected]

Eric Munson

University of Kentucky 789 S. Limestone Lexington, KY 40536 Tel: 859-323-3107 [email protected]

Joseph Murphy-Boesch

NIH, NINDS, LFMI 10 Center Drive Building 10, Room B1D728 Bethesda, MD 20892-1065 Tel: 301-594-2133 [email protected]

Dylan Murray

The Florida State University 96 Cheiftan Way Institute for Molecular Biophysics Tallahassee, FL 32306 Tel: 8506444145 [email protected]

Wazo Z. Myint

University of Pittsburgh 3501 Fifth, Ave. BST 3; Room B040 Pittsburgh, PA 15260 Tel: 267-408-1683 [email protected]

Rajakumar Nagarajan UCLA 10833 Le conte Ave CHS # BL 428 Los Angeles, CA 90095 Tel: 3102061629 [email protected]

Suryaprakash Nagarajarao

Indian Institute of Science NMR Research Centre Bangalore, Karnataka 560012 India Tel: 9.180229333e+011 [email protected]

Armando Navarro-Vázquez

Departamento de Quimica Organica. UVigo Facultade de Quimica. Lagoas Marcosende Vigo, Pontevedra 36210 Spain Tel: 34986812226 [email protected]

Gil Navon

Tel Aviv University Ramat Aviv Tel Aviv, Middle East 69978 Israel Tel: -6352199 [email protected]

Peter Neidig

Bruker BioSpin Silberstreifen Rheinstetten, DE-76287 Germany Tel: +49 721 5161 6447 [email protected]

Charlie Nelson

Agilent Technologies, Inc. 5301 Stevens Creek Blvd. Santa Clara, CA 95051 Tel: 650-553-3903 [email protected]

Sarah Nelson

UCSF Mission Bay Campus Byers Hall 1700 4th St,Rm 303, MC 2532 San Francisco, CA 94158-2330 [email protected]

Alexander A. Nevzorov

North Carolina State University Department of Chemistry North Carolina State Univ Raleigh, NC 27695 Tel: 919-515-3199 [email protected]

Bao D. Nguyen

Pfizer, Inc. 445 Eastern Point Road Groton, CT 06340 [email protected]

Da Qun Ni

Florida State University Tallahassee, FL 32309 Tel: 8509805456 [email protected]


Page 139

Walter P. Niemczura University of Hawaii 2545 McCarthy Hall Dept of Chemistry Honolulu, HI 96822 Tel: 808 956 3113 [email protected]

Yusuke Nishiyama

JEOL Resonance Inc. Musashino 3-1-2, Akishima Tokyo, 196-8558 Japan Tel: -2739 [email protected]

Gregory B. Norell


Theresa Norell

Norell, Inc. PO Box 307 Landisville, NJ 8326 [email protected]

Kristin Nuzzio

University of Illinois 600 S. Mathews Ave. MC-712 Box 84-6 Urbana, IL 61801 Tel: 9089309364 [email protected]

Eric Oldfield

University of Illinois 600 S. Mathews Urbana, IL 61801 Tel: 217 333 3374 [email protected]

Andrew Olson

NCSU 128 Polk Hall Raleigh, NC 27695 [email protected]

Dean Olson

Univ. of Illinois School of Chemical Sciences 600 S. Mathews Urbana, IL 61801 Tel: 217-244-0564 [email protected]

Ta-Chung Ong

Massachusetts Institute of Technology 170 Albany Street Francis Bitter Magnet Lab Cambridge, MA 02139 Tel: 206-434-7991 [email protected]

Beverly G Ostrowski

University of Minnesota 312 Church St. SE 6-155 Jackson Hall Minneapolis, MN 55455 Tel: 612-626-1148 [email protected]

Brian O'Sullivan Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CA 95051 [email protected]

Ann-Christin Pöppler

Georg August Universitat Gottingen TammannstraÃŸe 4 Gottingen, lower saxony 37077 Germany Tel: +49 551 3914444 [email protected]

Berit Paaske

Center for insoluble Protein Structures (inSPIN). Langelandsgade 140 Aarhus C, 8000 Denmark Tel: +45 87155376 [email protected]

Arthur G Palmer

Columbia University Biochemistry and Molecular Biophysics 630 West 168th Street New York, NY 10032 Tel: 212 305 8675 [email protected]

Anant Paravastu

Department of Chemical and Biomedical Engineering FAMU-FSU College of Engineering 2525 Pottsdamer St. Tallahassee, FL 32310 Tel: 240-643-9476 [email protected]

Teodor Parella

UAB Servei RMN Universitat Autonoma Barcelona Bellaterra, Barcelona 8193 Spain Tel: -935812257 [email protected]

Uresh Parikh

Merck & Co., RY 121-162 123 E. Scott ave Rahway, NJ 7065 Tel: 732-594-0474 [email protected]

Younghee Park

CCRC, University of Georgia Complex Carbohydrate Research Center 315 Riverbend Rd. Athens, GA 30602 Tel: 706-372-4026 [email protected]

Sudhakar Parthasarathy

Univ. of Illinois at chicago 845 W.Taylor St. Chicago, IL 60607 Tel: (312)576-5381 [email protected]

Horacio M. Pastawski Instituto de Fisica Enrique Gaviola Facultad de Matematica, Astronomia y Fisica Universidad Nacional de Cordoba Cordoba, 5000 Argentina Tel: 0054 351 5334051x264 [email protected]

Subhradip Paul

OSU 2332 Neil Avenue Apartment D Columbus, OH 43202 Tel: 8505913246 [email protected]

Joana Paulino

Institute of Molecular Biophysics FSU 91 Chieftan Way Tallahassee, FL 32306 Tel: 850-645-9474 [email protected]

Jeffrey Paulsen

Schlumberger-Doll Research One Hampshire St Cambridge, MA 02139 Tel: 617-768-2283 [email protected]

Eric K Paulson

Yale University 225 Prospect St, SCL 1 New Haven, CT 06511 Tel: 203-432-3942 [email protected]

Tim Peck

Agilent Technologies 5301 Stevens Creek Blvd. Santa Clara, CA 95051 [email protected]

Istvan Pelczer

Princeton University Washington Road Dept of Chemsitry, Frick Lab Princeton, NJ 8544 Tel: 609 258 2342 [email protected]

Perry J Pellechia

University of South Carolina Dept of Chemistry and Biochemistry 631 Sumter Street (GSRC) Columbia, SC 29208 Tel: 803 777-2088 [email protected]

Chen Peng

Mestrelab Research 1575 Tanglewood Ln, APT F-121 Escondido, CA 92029 Tel: 858 736 4563 [email protected]

Manuel Perez

Mestrelab Research Feliciano Barrere 9B-BX Santiago de Composta, 15706 Spain [email protected]


Page 140

Perttu Permi University of Helsinki Institute of Biotechnology, University of Helsinki P.O.Box 65, Viikinkaari 1 Helsinki, Helsinki FI-00014 Finland [email protected]

John Persons

Univ of Nebraska - Lincoln 724 Hamilton Hall Lincoln, NE 68588-0304 Tel: 4024729474 [email protected]

Ron Peterson

Daedalus Innovations LLC 3624 Market St., 5E Philadelphia, PA 19104 Tel: 267-499-2013 [email protected]

Katja Petzold

University of Michigan, Dept. Biophysics 930 N. University Av Ann Arbor, MI 48109 Tel: 734-834-1023 [email protected]

Richard Phan

US Army Dugway Proving Ground TEDT-DPW-CTE MS#4 4153 B Street Dugway, UT 84022 Tel: 435-831-7332 [email protected]

Francis Picart

Stony Brook University Department of Chemistry 100 John S. Toll Drive, Room 507 Stony Brook, NY 11794-3400 Tel: (631)632-7991 [email protected]

Giuseppe Pileio

University of Southampton School of Chemistry University Road Southampton, Hampshire SO171BJ UK Tel: 4.4238059415e+011 [email protected]

Guido Pintacuda

CNRS - ENS Lyon Centre de RMN a Tres Hauts Champs 5 rue de la Doua Lyon, Rhone-Alpes 69100 France Tel: 33633644687 [email protected]

Caroline D. Pointer-Keenan

University of Bayreuth Universitätsstraße 30 Bayreuth, Bayern 95440 Germany Tel: 4.9176507227e+012 [email protected]

Tatyana Polenova University of Delaware Department of Chemistry & Biochem 036 Brown Laboratory Newark, DE 19716 Tel: 302 831 1968 [email protected]

Simon Pondaven

The Ohio State University 1627 Elmwood Avenue Columbus, OH 43212 Tel: 6145935254 [email protected]

Katye Poole

University of Florida P.O. Box 117200 Gainesville, FL 32611 Tel: 3523924657 [email protected]

Richard J Porambo

Merck & Co., Inc. P.O. Box 4 WP78-107 West Point, PA 19486 Tel: 215-652-4144 [email protected]

Alexey Potapov

National Institute of Diabetes and Digestive and K 9000 Rockville Pike Bethesda, MD 20892 Tel: 3014024687 [email protected]

Mehrdad Pourfathi

University of Pennsylvania, Department of Radiolog 3450 Hamilton Walk, 338 Stemmler Hall Philadelphia, PA 19104 Tel: 215-662-6775 [email protected]

Robert Powers

University of Nebraska-Lincoln Department of Chemistry 722 Hamilton Hall Lincoln, NE 68588-0304 Tel: (402) 472-3039 [email protected]

Alexandra Pozhidaeva

UCONN Health Center 263 Farmington Ave Farmington, CT 06030-3305 Tel: 8606792769 [email protected]

Padmanava Pradhan

City University of New York Department of Chemistry 160 Convent Ave New York, NY 10031 Tel: 2126508266 [email protected]

Subramanian Prasad BASF Corporation 25 Middlesex-Essex TPK Iselin, NJ 8830 Tel: 732-205-5103 [email protected]

James H. Prestegard

University of Georgia CCRC, University ofGeorgia 315 Riverbend Rd Athens, GA 30602 Tel: 706-542-6281 [email protected]

John Price

PicoSpin LLC 5445 Conestoga Court, Suite 202 Boulder, CO 80301 Tel: 877 390 0465 [email protected]

Yulia Pustovalova

University of Connecticut Health Center 263 Farmington Ave Farmington, CT 06032 Tel: 860-679-2887 [email protected]

Qiao Qiao

university of South Florida 15501 Bruce B Downs Blvd Apt 2009 Tampa, FL 33647 Tel: 8134543078 [email protected]

Bao Qingjia

Huazhong Univ of Science and Tech Wuhan Institute of Physics and Math Chinese Academy of Sciences Wuhan, HuBei 430071 China Tel: 027-87199686 [email protected]

Feng Qiu

Bristol-Myers Squibb Co. 311 Pennington-Rocky Hill Road Pennington, NJ 18902 Tel: 609-818-4110 [email protected]

Yun Qu

VCU 1001 West Main St. Box 842006 Richmond, VA 23284-2006 Tel: 804-828-1934 [email protected]

Gregory Quinting

Anasazi Instruments 4101 Cashard Ave. #103 Indianapolis, IN 46203 Tel: 866-494-9369 [email protected]

Mukundan Ragavan

Texas A&M University Department of Chemistry College Station, TX 77843 Tel: 9798624240 [email protected]


Page 141

S. Raghothama Indian Institute of Science NMR Research centre Indian Institute of Science Bangalore, karnataka 560012 India Tel: +91 80 22933301 [email protected]

Srinivasan Rajan

Novartis Institutes for BioMedical Research, Inc., #600-6C-172 250 Massachusetts Avenue Cambridge, MA 02139 Tel: 617-871-3425 [email protected]

Paul Ralifo

Boston University 590 Commonwealth Avenue Chemistry Dept Boston, MA 02215 Tel: 617 353 4818 [email protected]

Belen RamÃ-rez-Cordero

UNAM Circuito Exterior s/n Ciudad Universitaria Mexico, D.F. 4510 Mexico Tel: 15556224613 [email protected]

Vijaykumar Ramaswamy

University of Florida 1600 SW Archer Road ARB R3-234 Gainesville, FL 32610 Tel: 352-392-3109 [email protected]

Mark Rance

Dept. of Molecular Genetics, Biochemistry and Micr 231 Bethesda Avenue University of Cincinnati Cincinnati, 0 45267-0524 Tel: 513 558 0066 [email protected]

Kaili Ranta

SIUC 2012 S. Illinois Ave, Apt #18 Carbondale, IL 62903 Tel: 6513237393 [email protected]

Dale Ray

Case Western Reserve University Dept. of Chemistry 10900 Euclid Ave LC=7078 Cleveland, OH 44106-7078 Tel: 216 368-2404 [email protected]

Joseph Ray

Baxter Healthcare 25212 W. Illinois Route 120 WG3-1S Round Lake, IL 60073 Tel: 847-270-6876 [email protected]

G Jithender Reddy Tata Institute of Fundamental Research Homi Bhabha Road-1, Navy nagar Colaba Mumbai, Maharastra 400005 India Tel: -9987910049 [email protected]

Marcel Reese

Massachusetts Institute of Technology 170 Albany Street Cambridge, MA 02139 Tel: -3880 [email protected]

Jeffrey Reimer

UC Berkeley 201 Gilman Hall Berkeley, CA 94720 Tel: 510-642-8011 [email protected]

Xiaobai Ren

Sanford-Burnham Medical Research Institute 6400 Sanger Road Orlando, FL 32827 Tel: 203-889-8316 [email protected]

Bob Repke

SP Scientific 3538 Main Street Stone Ridge, NY 12484 Tel: 845 255 5000 [email protected]

William F Reynolds

University of Toronto Department of Chemistry 80 St. George St Toronto, ON M5S 3H6 Canada Tel: (416) 9783563 [email protected]

Anthony A Ribeiro

Duke University Duke NMR Center, B143 LSRC Bldg. Research Drive Durham, NC 27710 Tel: 919 613 8887 [email protected]

David M. Rice

Agilent Technologies 5301 Stevens Creek Blvd 2U-C011 Santa Clara, CA 95051 Tel: 408-553-4438 [email protected]

David Richardson

Univ of Central Florida PO Box 162366 Orlando, FL 32816 Tel: 407 823 2961 [email protected]

Clark D. Ridge University of Miami Department of Chemistry University of Miami Coral Gables, FL 33124 Tel: (305) 284-1847 [email protected]

Chad Rienstra

University of Illinois 600 South Mathews Avenue Box 50-6, MC 712 Urbana, IL 61801 Tel: 217 244-4655 [email protected]

Milagros Rifkind

Agilent Technologies 2850 Centerville Rd Wilmington, DE 19808 Tel: 302 633 8582 [email protected]

Scott Riley

Tecmag 10161 Harwin, #150 Houston, TX 77479 Tel: 713 667 8747 [email protected]

Peter L. Rinaldi

The University of Akron Department of Chemistry Akron, OH 44325-3601 Tel: 330-972-5990 [email protected]

William M. Ritchey

851 Haywood Drive South Euclid, OH 44121-3403 [email protected]

Emily Ritz

University of Guelph 50 Stone Rd East Guelph, ON N1G 2W1 Canada [email protected]

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University of South Florida 4202 E Fowler Ave, CHE 205 Tampa, FL 33620 Tel: 813-974-0013 [email protected]

Margaret Roberts


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Page 142

Melanie M Rosay Bruker BioSpin Corporation 15 Fortune Drive Billerica, MA 01821 Tel: 978-667-9580 [email protected]

Matthew Rosen

Harvard University/Martinos Center for Biomedical Department of Physics 17 Oxford Street Cambridge, MA 02138 Tel: (617) 643-8636 [email protected]

Ke Ruan

School of Life Science, University of Science and 443 Huangshan Road Hefei, Anhui 230027 China Tel: +86 0551 3607767 [email protected]

Dave Russell


Randy D. Rutkowske

GlaxoSmithKline 5 Moore Dr RTP, NC 27709 Tel: 919 483 6078 [email protected]

Yaroslav Ryabov

National Institutes of Health 12A/2041, South Drive, MSC 5624 Bethesda, MD 20892 Tel: (301) 435 9034 [email protected]

Joseph Sachleben

Univ of Chicago 929 E 57th St Chicago, IL 60637 Tel: 773-834-9866 [email protected]

Dimitrios Sakellariou

CEA Saclay DSM/IRAMIS/SIS2M/LSDRM CEA Saclay Gif-Sur-Yvette, Ile de France 91191 France Tel: +33 1 69081126 [email protected]

Qasim Saleem

University of Toronto Department of Chemical and Sciences, 3359 Mississauga Road N. Mississauga, ON L5L 1C6 Canada [email protected]

Loic Salmon University of Michigan 930 N. University Ann Arbor, MI 48109 Tel: 7342392244 [email protected]

Nicola Salvi

Ecole Polytechnique Federale de Lausanne EPFL ISIC BCH 1532 Lausanne, Vaud 1015 Switzerland [email protected]

Mônica Santos de Freitas

UFRJ Av. Carlos Chagas Filho 373, Ilha do Fundao, CCS, Bloco K, CNRMN Rio de Janeiro, Rio de Janeiro 21941-902 Brazil [email protected]

Partha Sarathy

Texas A&M University Department of Chemistry Texas A&M University College Station, TX 77842-3012 Tel: 979 458 0705 [email protected]

Maziar Sardashti

ConocoPhillips 178-PL, BTC Bartlesville, OK 74004 Tel: 918-661-4129 [email protected]

Mariana Sardo

University of Aveiro Chemistry Department Campus de Santiago Aveiro, Aveiro 3810-193 Portugal Tel: 3.5196353093e+011 [email protected]

Carolina Sarzedas

Federal University of Rio de Janeiro Av Carloa Chagas Filho,373 - CCS - Bloco H - Lab. H010 Rio de Janeiro, Rio de Janeiro 21941-902 Brazil Tel: (+55)(21)2562-6793 [email protected]

Hiroaki Sasakawa

JEOL UK JEOL House, Silver Court, Watchmead Welwyn Garden City, Europe AL71LT UK [email protected]

Ryan R. Sasaki

ACD/Labs 8 King Street East, Suite 107 Toronto, ON M5C 1B5 Canada Tel: 416-368-3435 x299 [email protected]

Hajime Sato

Bruker Biospin KK Japan 3-9 Moriya Kanagawa Yokohama, 221-0022 Japan [email protected]

EmmaLou Satterfield Missouri Univ of Science & Technology 400 W. 11th Street Rolla, MO 65409-0001 Tel: 573-341-7654 [email protected]

Ulrich Scheler

Leibniz-Institut fur Polymerforschung Dresden e.V. Hohe Str. 6 Dresden, Saxony D-01069 Germany Tel: (011) 49 351 4658 275 [email protected]

Thomas Schmid

RUAG Space Stachegasse 16 Vienna, 1120 Austria Tel: 43 1 801 199 2200 [email protected]

Christopher Schmidt

University of South Carolina 315 Main Street Columbia, SC 29208 Tel: 8032367116 [email protected]

Celine Schneider

Memorial University of Newfoundland C-CART Memorial University of Newfoundland St John's, NL a1b3x7 Canada Tel: 1-709-864-3134 [email protected]

Regina Schuck


Matthias Schulze

Euriso-Top GmbH Lebacher Str. 4 Saarbrucken, 66113 Germany Tel: +49 681 9963338 [email protected]

Robert W. Schurko

University of Windsor 401 Sunset Ave. Windsor, ON N9B3P4 Canada Tel: 519-253-3000 3548 [email protected]

Harald Schwalbe

Univ of Frankfurt Institute of Organic Chemistry Frankfurt, D-60438 Germany Tel: 49 6979829737 [email protected]

Herb Schwartz

Dept of Chemistry and Biological Chemi Rensselaer Polytechnic Institute 110 N. 8th St Troy, NY 12180 Tel: 518-276-6779 [email protected]


Page 143

Charles Schwieters National Institutes of Health 12A/2041, National Institutes of Health 12 South Drive, MSC 5624 Bethesda, MD 20892 Tel: 301-402-4914 [email protected]

Ishita Sengupta

Graduate Student 1073 Evans Laboratory, 100 W 18th Avenue Columbus, OH 43210 Tel: 6142927653 [email protected]

Jeff Seymour

Mestrelab Research 1 Oakland View Oaklands Welwynn, Herts AL5 ORJ UK Tel: 44 1438717217 [email protected]

Nikolaos Sgourakis

University of Washington Department of Biochemistry Seattle, WA 98105 Tel: 5185283385 [email protected]

Astghik Shahkhatuni

Molecule Structure Research Center Azatutyan 26 Yerevan, 14 Armenia Tel: 37494134135 [email protected]

A. J. Shaka

Univ of California Dept of Chemistry Irvine, CA 92617-4054 Tel: 949 824 8509 [email protected]

Michael Shapiro

Pfizer 558 Eastern Point Road groton, CT 06340 [email protected]

Fiana Shaw

Cambridge Isotope Lab 50 Frontage Rd Andover, MA 01810 [email protected]

Lu Shen

UCLA c/o Yung-Ya Lin group, 1032 Young Hall, Dept of Chemistry and Biochemistry, 607 Charles E. Young Drive East Los Angeles, CA 90095-1569 Tel: (310)993-7489 [email protected]

Devon Sheppard

University of Oxford South Parks Rd Oxford, OX1 3RE UK Tel: +44 0758 413 4466 [email protected]

Junhui Shi Princeton Univeristy B22 Jadwin Hall Princeton, NJ 8540 Tel: 6099377036 [email protected]

Xiangyan Shi

Dept of Chemistry and Biochemistry University Drive and Mill Avenue Arizona State University Tempe, AZ 85287-1604 Tel: 4803041450 [email protected]

Nahoko Shimokawa


Chang Shin

University of California Department of Chemistry University of California Berkeley, CA 94720 Tel: 510-847-5529 [email protected]

Shoji Shiota


Scott Showalter

The Pennsylvania State University 104 Chemistry Building University Park, PA 16802 Tel: 8148652318 [email protected]

Matsyendra Nath Shukla

Indian Institute of Science Education & Research (IISER) Knowledge City Sector 81 SAS Nagar PO Manauli Mohali, Punjab 140306 India Tel: 9.184278193e+011 [email protected]

Ting Ann Siaw

University of California Santa Barbara Department of Chemical Engineering, Santa Barbara, CA 93106 Tel: 805-252-9490 [email protected]

Sarmad Siddiqui

University of Pennsylvania 4418 Spruce St #D4 Philadelphia, PA 19104 [email protected]

Viviane Silva de Paula

Federal University of Rio de Janeiro Av Carlos Chagas Filho 373, UFRJ - CCS - BL K - ANEXO Rio de Janeiro, Rio de Janeiro 21941-590 Brazil [email protected]

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Carnegie Mellon University 4400 Fifth Ave Pittsburgh, PA 15213 Tel: 412 268 1990 [email protected]

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Carnegie Mellon University 4400 Fifth Ave Pittsburgh, PA 15213 Tel: 412 268 4081 [email protected]

Andre J Simpson

University of Toronto 1265 Military Trail Toronto, ON MIC1A4 Canada Tel: 416 287 7547 [email protected]

Myrna J. Simpson

University of Toronto Department of Chemistry 1265 Military Trail Toronto, ON M1C1A4 Canada Tel: 416-287-7234 [email protected]

Nadia Singh

University of the West Indies 19A Seaview Gardens Carenage, West Indies 0 Trinidad and Tobago Tel: 868-795-4844 [email protected]

Jagadishwar Sirigiri

Bridge12 Technologies Inc. 37 Loring Drive Framingham, MA 01702 Tel: 617-674-2766 [email protected]

Jerzy Sitkowski

National Medicines Institute Chelmska 30/34 Warsaw, 00-725 Poland Tel: 48 22 8514372 [email protected]

Nikolai R. Skrynnikov

Purdue University Department of Chemistry 560 Oval Drive West Lafayette, IN 47907-2084 Tel: 765 494 8519 [email protected]


Page 144

Alex I. Smirnov North Carolina State University Department of Chemistry, Box 8204 2620 Yarbrough Drive Raleigh, NC 27695-8204 Tel: 1-919-513-4377 [email protected]

Vadim Smirnov

Optigrate Corp. 3267 Progress Drive Orlando, FL 32826 [email protected]

Denise Smith

Wilmad LabGlass 1172 NW BLVD Vineland, NJ 8360 Tel: 856 697 3000 [email protected]

Karen Ann Smith

University of New Mexico Dept of Chemistry & Chemical Biology University of New Mexico MSCO 3 2060 Albuquerque, NM 87131 Tel: 505-277-4031 [email protected]

Luis J. Smith

Clark University Department of Chemistry 950 Main St. Worcester, MA 01610 Tel: (508) 793-7753 [email protected]

Pieter Smith

Weizmann Institute of Science Chemical Rehovot, 76100 Israel [email protected]

Steven O. Smith

Stony Brook University Center for Structural Biology Stony Brook, NY 11794-5115 Tel: 631-632-1210 [email protected]

Yi-Qiao Song

Schlumberger 1 Hampshire Street Cambridge, MA 02139 Tel: 203 470 4816 [email protected]

Ronald Soong

University of Toronto 1236 Military Trails Toronto, ON M1C1A4 Canada Tel: 416-208-2949 [email protected]

Lindsay Sperling

Lawrence Berkeley National Laboratory 1 Cyclotron Rd Bldg. 922-208C Berkeley, CA 94720 Tel: 510-642-2094 [email protected]

Leonard D. Spicer Duke University Biochemistry Box 3711, DUMC Durham, NC 27710 Tel: 919-684-4327 [email protected]

Hans W. Spiess

Max Planck Institute Polymers P.O. Box 3148 Mainz, 55021 Germany Tel: -385202 [email protected]

Manfred Spraul


Manfred Spraul


John Staab


Donald Stec

Vanderbilt University 7300 Stevenson Center Nashville, TN 37122 Tel: 615-322-6704 [email protected]

Rachel Steinle

Bruker BioSpin 15 Fortune Drive Billerica, MA 01821 Tel: 978-944-8615 [email protected]

Carlos Steren

Dept. of Chemistry Univ of Tennessee, Buehler Hall Knoxville, TN 37996 Tel: 865-974-3386 [email protected]

Richard J. Stevens

Stelar/Molecular Specialties 10437 Innovation Dr., #301 Milwaukee, WI 53226 Tel: 414-258-6724 [email protected]

Mikaela Stewart

Dept of Biochemistry and Biophysics, Texas A&M Uni Biochemistry/Biophysics 130 Olsen Blvd College Station, TX 77843-2128 Tel: 979-845-6313 [email protected]

Neal J Stolowich University of Louisville Department of Chemistry 2320 S. Brook Street Louisville, KY 40292 Tel: (502) 852-7894 [email protected]

Sean Stowe


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Agilent Technologies 5301 Stevens Creek Blvd Santa Clara, CO 95051 [email protected]

Henry J. Stronks

Bruker BioSpin Canada 555 Steeles Ave East Milton, ON L9T 1Y6 Canada Tel: 905 876 4641 [email protected]

Jochem Struppe

Bruker-Biospin 15 Fortune Drive Billerica, MA 01821 Tel: 978 973 3547 [email protected]

Dirk Stueber

Merck & Co., Inc. 126 East Lincoln Avenue, RY 818-B112 P.O. Box 2000 Rahway, NJ 7065 Tel: 732-594-8852 [email protected]

Biing-Ming Su

Akzo Nobel Surface Chemistry, LLC 281 Fields Lane Brewster, NY 10509 Tel: 845-276-8292 [email protected]

Hiroto Suematsu

JEOL Resonance Inc. 3-1-2 Musashino, Akishima Tokyo, 196-8558 Japan Tel: 042-543-1111 [email protected]

Christopher Suiter

University of Delaware 207 Wharton Dr. Newark, DE 19711 Tel: 828-308-6204 [email protected]


Page 145

Shangjin Sun Structural Biophysics Laboratory, National Cancer 538 Chandler Street Frederick, MD 21702 Tel: 3018466452 [email protected]

Sandip Sur

U of Rochester 6 Frederick Rd Pittsford, NY 14534 Tel: 5852754705 [email protected]

Dieter Suter

Universitat Dortmund Fakultat Physik TU Dortmund Dortmund, 44221 Germany Tel: +49 231 755 3512 [email protected]

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Stanislav Sykora

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Vanderbilt University 7330 Stevenson Center Station B 351822 Nashville, TN 37235 Tel: 615-322-6074 [email protected]

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JEOL Resonance Inc. 1-2 Musashino 3-chome Akishima city Tokyo, 196-8558 Japan Tel: +81 42-542-2236 [email protected]

C.T. Tan


Huiru Tang Wuhan Institute of Physics and Mathematics 30 Xiaohongshan West Chinese Academy of Sciences Wuhan, Hubei Province 430071 China Tel: -87198371 [email protected]

Joel A Tang

NHMFL FSU 1800 E Paul Dirac Dr, Rm 203B Tallahassee, FL 32310 Tel: 850-644-1300 [email protected]

Ming Tang

University of Illinois at Urbana-Champaign A127B CLSL Box# 41-6 Department of Chemistry 600 S Mathews Ave Urbana, IL 61801 Tel: 217-244-1583 [email protected]

Mitsuru Tashiro

Meisei University 2-1-1 Hodokubo Hino, Tokyo 191-8506 Japan Tel: -6149 [email protected]

Gopinath Tata

University of Minnesota 5-256 Hasselmo Hall 312 Church St SE Minneapolis, MN 55455 Tel: 6124231432 [email protected]

Francis Taulelle

Univ. Versailles Tectospin, Institut Lavoisier, CNRS UMR 8180 45 Avenue des Etats-Unis Versailles Cedex, Ile de France 78035 France Tel: 33139254477 [email protected]

William Tay

Mayo Clinic 13810 Sutton Park Dr N Apt#234 Jacksonville, FL 32224 [email protected]

Fariba Tayyari

Purdue University 135 Nimitz Drive apt#10 West lafayette, IN 47906 Tel: 765-212-4821 [email protected]

Razvan Teodorescu

Bruker BioSpin Corp. 15 Fortune Drive Billerica, MA 01821 Tel: 978-667-9580 ext. 5378 [email protected]

Marc Ter Horst University of North Carolina Department of Chemistry 131 South Road, Caudill Labs, 056 Chapel Hill, NC 27599-3290 Tel: 919-843-5802

Richele Thompson


Brent Thorn

New Era Enterprises PO Box 747 Vineland, NJ 8362 [email protected]

Scott Thornburgh

Dow Agrosciences 9330 Zionsville Road Building 306/E1 Indianapolis, IN 46268 Tel: 3173373418 [email protected]

Pierre Thureau

Institut de Chimie Radicalaire Aix-Marseille University Marseille, F 13013 France Tel: 33491288578 [email protected]

Suhas Tikole

Institute of Biophysical Chemistry Goethe University Max-von-Laue-Str. 9 Frankfurt (Main), Hessen 60438 Germany Tel: 49 69 798 29670 [email protected]

Luzineide Tinoco

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Nico Tjandra

National Institutes of Health 50 South Drive Bld 50, Room 3503 Bethesda, MD 20892 Tel: 301-402-3029 [email protected]

Hidehito Tochio

Kyoto University Nishikyo-ku Kyoto, Kyoto Prefecture 615-8510 Japan Tel: -2913 [email protected]


Page 146

Tatsuhiro Tokunaga Astellas Pharma Inc. 21 Miyukigaoka Tsukuba-shi, Ibaraki 305-8585 Japan Tel: -7294 [email protected]

John Trail

Magritek 32 Salamanca Road Wellington, 6012 New Zealand Tel: 64 4 9207 671 [email protected]

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UCCS-CNRS UMR8181-Univ Lille1 Batiment C7UCCS UMR CNRS 8181Avenue Dimitri Me, BP 108 Villeneuve d'Ascq Cedex, 59 59652 France Tel: +(33).3.20.33.59.07 [email protected]

Milton Truong

Vanderbilt Univ Inst of Imaging Science 1161 21st Avenue South Medical Center North, AA-1105 Nashville, TN 37232-2310 [email protected]

Shigenori Tsuji

JEOL Resonance Inc. 3-1-2 Musashino Akishima, Tokyo, 81-42-544-1955 Japan Tel: 81-42-542-2236 [email protected]

Yu Tsutsumi

JEOL Resonance Inc. 1-2 Musashino 3-Chome Akishima, Tokyo, 196-8558 Japan [email protected]

Ashley Tucker


Flaviu R. Turcu

Pacific Northwest National Laboratory 902 Battelle Blvd. Richland, WA 99354 Tel: 1.1074481873e+011 [email protected]

Gary Turner

Spectral Data Services, Inc. 818 Pioneer St. Champaign, IL 61820 Tel: 217-352-7084 [email protected]

Ted Turner

Spectral Data Services, Inc. 818 Pioneer St. Champaign, IL 61820 Tel: 2173527084 [email protected]

Marcus Tuttle University of Illinois 600 South Mathews Avenue MC-712 Box 78-6 Urbana, IL 61801 Tel: 2172441583 [email protected]

Robert Tycko

National Institutes of Health Building 5, Room 112 Bethesda, MD 20892-0520 Tel: 301-402-8272 [email protected]

Sergiy Tyukhtenko

Northeastern University CDD, 36 Hurtig Hall 360 Huntington Av. Boston, MA 02115 Tel: 617-373-4219 [email protected]

Obehi Ukpebor

Hunter College of CUNY Dept of Physics 695 Park Ave New York, NY 10065 Tel: 347 720 7446 [email protected]

Stefan Ulmer

ASACUSA - AD03 Building 506/R-023 European Organization for Nuclear Research CERN Geneve 23, CH-1211 Switzerland [email protected]

Ilker Ün

Gebze Institute of Technology Chemistry Department Gebze, Kocaeli 41400 Turkey Tel: 9.0532301298e+011 [email protected]

Marcel Utz

University of Virginia Department of Mechanical and Aerospace Engineering Charlottesville, VA 22904 Tel: 434 243 4098 [email protected]

Homayoun Valafar

University of South Carolina Swearingen Engineering center 315 Main Street Columbia, SC 29208 Tel: 803-777-2404 [email protected]

Mark Van Criekinge

UCSF - Radiology Mission Bay Campus 1700 4th Street San Francisco, CA 94158 Tel: 415-476-3432 [email protected]

Rob Van Daalen Elsevier Radarweg 29 Amsterdam, 1043 NX Netherlands Tel: +31-20-485 2206 [email protected]

Patrick C.A. van der Wel

University of Pittsburgh 3501 Fifth Ave BST3 2044 Pittsburgh, PA 15260 Tel: 412-3839896 [email protected]

Ernst van Eck

Radboud University Nijmegen Solid State NMR Heyendaalseweg 135 Nijmegen, 6525AJ Netherlands Tel: 31243653105 [email protected]

Murugendra Vanarotti

St Jude Children's Research Hospital 262 Danny Thomas Place Memphis, TN 38105 Tel: 901-595-6399 [email protected]

Krisztina Varga

University of Wyoming 1000 E. University Ave Laramie, WY 82071 Tel: 307-7611748 [email protected]

David Vargas

Bruker Biospin 15 Fortune Drive Billerica, MA 01821 Tel: 9784309872 [email protected]

Andrew Varney

Agilent Technologies UK Ltd The Magnet Technology Centre 6 Mead Road, Yarnton, Oxford, Oxon. OX5 1QU UK Tel: +44 1865 853835 [email protected]

Kristen Varney

University of Maryland, School of Medicine 4932 Brampton Pkwy Ellicott City, MD 21043 Tel: 410-706-2110 [email protected]

Michele Vendruscolo

University of Cambridge Department of Chemistry Lensfield Road Cambridge, Cambridgeshire CB2 1EW UK Tel: +44 1223 763873 [email protected]


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Aurélie Vicente LCS - Universite de CAEN 6 bd Marechal Juin CAEN, Basse Norandie 14000 France Tel: 33 (2) 31 45 28 16 [email protected]

Stéphane Viel

Aix-Marseille Univ. & CNRS, ICR UMR 7273 Centre de Saint Jerome, case 512 Av. Escadrille Normandie Niemen Marseille, PACA 13397 cedex 20 France Tel: +33 (0) 4 91 28 8902 [email protected]

Daniel B Vigneron

University of California Dept of Radiology UCSF Box 2512 San Francisco, CA 94158 Tel: 415-476-3343 [email protected]

Lisa Vingara

Oregon Health and Science University 2202 SW Bertha Blvd., Apt 7 Portland, OR 97239 [email protected]

Joachim M. Vinther

Interdisciplinary Nanoscience Center, Aarhus Unive Department of Chemistry Langelandsgade 140 Aarhus, DK-8000 Denmark Tel: 4522164913 [email protected]

Thomas Vosegaard

University of Aarhus Aarhus School of Engineering Langelandsgade 140 Aarhus, Aarhus 8000 Denmark Tel: 4587155929 [email protected]

Liliya Vugmeyster

University of Alaska Anchorage Department of Chemistry, UAA 3211 Providence Dr Anchorage, AK 99508 Tel: 907-7864709 [email protected]

George Wagner

U.S. Army ECBC 5813 Blackhawk Rd. Attn: RDCB-DRP-F APG, MD 21010-5424 Tel: (410) 436-8468 [email protected]

Gerhard Wagner

Dept. Biol. Chem. & Mol. Pharmacologie Harvard Medical School 240 Longwood Avenue Boston, MA 02115 Tel: 617-432-3213 [email protected]

Larry Wald MGH NMR Core at Martinos Center Building 75, Room 2.109 13th Street Charlestown, MA 02129 [email protected]

Brennan Walder

Ohio State 1350 King Avenue, Apt 109 Columbus, OH 43212 Tel: 715-630-9672 [email protected]

Laura L. Walkup

Southern Illinois University Carbondale 1245 Lincoln Drive, 201 Neckers Hall Carbondale, IL 62901-4409 Tel: 618 453 6266 [email protected]

Joshua Wand

Univ of Pennsylvania Dept of Biochemistry & Biophysics 905 Stellar-Chance Labs Philadelphia, PA 19104-6059 Tel: 215-573-7288 [email protected]

Connie Wang

JS Research, Inc. 366 Manet Avenue Quincy, MA 02169 Tel: 617 786 0939 [email protected]

Jin-Shan Wang

JS Research, Inc. 366 Manet Avenue Quincy, MA 02169 Tel: 617 786 0939 [email protected]

Miao Wang

Wilmad LabGlass 1172 NW BLVD Vineland, NJ 8360 Tel: 856 691 3200 [email protected]

Tianzhi Wang

University of Texas Medical Branch 301 University Blvd NMR dockside bldg, room 1.104 Galveston, TX 77555-1157 Tel: 409-747-6821 [email protected]

Tuo Wang

Department of Chemistry Iowa State University Ames, IA 50011 [email protected]

Yingzi Wang

Bristol-Myers Squibb 5 Research Parkway Wallingford, CT 06492 Tel: 2036775742 [email protected]

Yulan Wang Wuhan Institute of Physics and Mathematics 30 West Xiao-Hong-Shan Wuchang District Wuhan, Wuchang 430071 China Tel: 00-86-13407137086 [email protected]

Mieng-Hua Wann

Forest Laboratories Inc. 45 Adams Avenue Hauppauge, NY 11788 Tel: 631-436-2608 [email protected]

Jorg Warchtrup

Universitat Stuttgart 3. Physikalisches Institut Pfaffenwaldring 57 Stuttgart, 70569 Germany [email protected]

Warren S. Warren

Duke University Center for Molecular and Biomolecular Imaging Box 90346 Durham, NC 27712 Tel: 919-660-1604 [email protected]

Dror E. WARSCHAWSKI

CNRS IBPC 13 rue Pierre et Marie Curie Paris, Paris 75005 France Tel: (33) 1 58 41 51 11 [email protected]

Nancy Washton

Pacific Northwest National Laboratory 902 Battelle Boulevard, MSIN K8-98 Richland, WA 99352 Tel: 509 371 7094 [email protected]

Christian Wasmer

Harvard Medical School 240 Longwood Ave Boston, MA 02115 Tel: 8574990131 [email protected]

Miki Watanabe

Claflin University 898 Goff st Orangeburgh, SC 29115 [email protected]

Jan Watzlaw

Institute of Materials in Electrical Engineering 1 Sommerfeldstr. 24 Aachen, 52074 Germany Tel: 21402 [email protected]


Page 148

Gerard Weatherby CONNJUR 10 Townline Road Windsor Locks, CT 06096 Tel: 8603352375 [email protected]

Jon Webb

MR Resources, Inc. 160 Authority Drive Fitchburg, MA 01420 Tel: 978 345 9010 [email protected]

Sebastian Wegner


Jia Wei

Bruker BioSpin 11 South Zhong Guan Cun Street Room 5216, Everbright Int'l Trust Mansion Beijing, Asia Pacific 100081 China Tel: +86-10-6847 2030 [email protected]

Markus Weingarth

Universiteit Utrecht Bijvoet Center for Biomolecular Research Padualaan 8 Utrecht, 3584 Netherlands Tel: +31(0)30-2532875 [email protected]

Parris Wellman

T2 Biosystems 101 Hartwell Ave. Lexington, MA 02421 [email protected]

Patrick Wheeler

ACD Labs 8 King Street East, Suite 107 Toronto, ON M5C 1B5 Canada Tel: 416 368 3435 [email protected]

Nicholas Whiting

SPMMRC; U. of Nottingham 10 Marina Avenue Nottingham, Nottinghamshire NG9 1HB UK Tel: (044) 790 650 0342 [email protected]

Sean Whittier

Yale University 350 Edwards St. New Haven, CT 06511 Tel: 203-432-5728 [email protected]

David Wilson

UCSF 1700 4th St. Byers Hall 203 San Francisco, CA 94158 Tel: (415)305-2295 [email protected]

Kimberly Wilson University of Notre Dame 251 Nieuwland Science Hall Notre Dame, IN 46556 Tel: 574-631-0285 [email protected]

Erick Winston

picoSpin LLC 5445 Conestoga Court, Suite 202 Boulder, CO 80301 [email protected]

Raiker Witter

TUT Ehitajate tee 5 Tallinn, 19086 Estonia Tel: 49-7247-82-3944 [email protected]

Klaus Woelk

Missouri S&T Department of Chemistry 400 W 11th Street Rolla, MO 65409-0010 Tel: +1 573 341 4432 [email protected]

Dennis Wolfel


Gerd Wolff

Bruker BioSpin GmbH Silberstreifen 4 Rheinstetten, DE-76287 Germany Tel: +49 721 5161-6211 [email protected]

Kurt F Wollenberg

Lubrizol Corporation 29400 Lakeland Blvd Wickliffe, OH 44092 Tel: 440 347-2026 [email protected]

Ryan Wood

University of Florida Department of Chemistry New Physics Building Corner of Gale Lemerand Dr and Museum Rd Gainesville, FL 32611 Tel: 301-643-3729 [email protected]

Bainan Wu

Sanford-Burnham Medical Research Inst 10901 North Torrey Pines Road La Jolla, CA 92037 Tel: 858-646-3100 [email protected]

Chin H. Wu

University of California, San Diego 9500 Gilman Drive, MC 0127 La Jolla, CA 92093 Tel: 858 822 5932 [email protected]

Donghui Wu Colgate-Palmolive Company 909 River Road Piscataway, NJ 8854 Tel: 7328786189 [email protected]

Jian Wu

The Dow chemical Co. Core R&D, Analytical Sciencies 727 Norristown Road Spring House, PA 19477-0904 Tel: (215) 641-7081 [email protected]

Shaoxiong Wu

Emory University 1515 Dickey Drive Atlanta, GA 30322 Tel: 404 727 6621 [email protected]

Yuyang Wu

Northwestern Univ 2145 Sheridan Road Evanston, IL 60208 Tel: 847-491-7080 [email protected]

Wei Wycoff

University of Missouri 601 S. College Ave. 125 Chemistry Building Columbia, MO 65211 Tel: 573-884-7807 [email protected]

Youlin Xia

University of Minnesota Biochem, Molec Biol/Biophysics Room 6-155 JacH Minneapolis, MN 55455 Tel: 612-626-3805 [email protected]

Yiling Xiao

Univ. of Illinois at Chicago Department of Chemistry 845 West Taylor Street - MC 111 Chicago, IL 60607 Tel: 312 4132943 [email protected]

Li Xie

Michigan State University Rm 42, Chemistry building Michigan State University East Lansing, MI 48824 Tel: 517-492-7242 [email protected]

Qiuwei Xu

Merck Research Laboratories 770 Sumneytown Pike WP81-205 West Point, PA 19486 Tel: 215-652-6004 [email protected]


Page 149

Xiang Xu New York University 31 Washington Pl Dept of Chemistry, Rm 1001 New York, NY 10003 Tel: 212-998-8463 [email protected]

Liang Xue

Alcon labs 6201 South Freeway, R3-18 Fort Worth, TX 76134 Tel: 817-551-8001 [email protected]

Yi Xue

Purdue University 204 Airport Rd Apt 9 West Lafayette, IN 47906 Tel: 765-496-3324 [email protected]

Si Yan

University of Delaware Brown Lab, 041 Newark, DE 19716 Tel: 302-831-8624 [email protected]

Fei Yang

Miami University 701 E High Steet Oxford, OH 45056 Tel: 5135293163 [email protected]

Shan Yang

University of Michigan 2016 Medford Rd Apt #31 Ann Arbor, MI 48104 [email protected]

Shengtian Yang

Novartis 4560 Horton Street Emeryville, CA 94608 Tel: 5109232757 [email protected]

Yuan Yang

Colorado School of Mines 1500 Illinois Str. Chemistry and Geochemistry Department Golden, CO 80401 Tel: 3033842109 [email protected]

Yunhuang Yang

Miami University 701 E High Street Dept of Chemistry and Biochemistry Oxford, OH 45056 Tel: 5135292813 [email protected]

Jeffery L Yarger

Arizona State University Dept of Chemistry and Biochemistry PO Box 871604 Tempe, AZ 85287 Tel: 480-399-7705 [email protected]

Chaohui Ye Wuhan Institute of Physics and Mathematics (WIPM), West No.30 Xiao Hong Shan, Wuchang, Wuhan, Hubei 430071 China Tel: 027-87197114 [email protected]

Weihua Ye

Stockholm University Svante Arrhenius vag 16C Stockholm, SE-106 54 Sweden Tel: +46 8 162447 [email protected]

Yueqi Ye

JEOL Resonance Inc. 1-2 Musashino 3-chome Tokyo, Akishima-shi 196-8558 Japan Tel: 81425422241 [email protected]

Xiyu Yi

University of California, Los Angeles 405 Hilgard Ave Los Angeles, CA 90095 Tel: 310-498-0368 [email protected]

Masashi Yokochi

Hokkaido University N-12, W-6, Kita-ku Sapporo, Hokkaido 001-0021 Japan Tel: -9645 [email protected]

Yasunao Yokota

JASTEC 5-9-12 Kitashinagawa, Shinagaw-Ku Tokyo, 141-8688 Japan Tel: 81 3 5739 5210 [email protected]

Bingwu Yu

CBER/FDA 8800 Rockville Pike Room130/building 29 Bethesda, MD 20892 [email protected]

Liping Yu

University of Iowa B291 CBRB University of Iowa Iowa City, IA 52242 Tel: 319-384-3172 [email protected]

Tairan Yuwen

Purdue University 560 Oval Drive Box 840 West Lafayette, IN 47907 Tel: 7654963324 [email protected]

Jaroslav Zajicek

University of Notre Dame 139 Nieuwland Hall Dept of Chemistry Notre Dame, IN 46556 Tel: 574 631 9111 [email protected]

Toby Zens Agilent Technologies 5301 Sevens Creek Blvd Santa Clara, CA 95051 Tel: 408 553 4166 [email protected]

Boyang Zhang

New York University Department of Chemistry New York University New York, NY 10003 [email protected]

Chunxin Zhang

GE Global Research 1 Research Circle Niskayuna, NY 12309 Tel: 1 518387 7642 [email protected]

Fengli Zhang

NHMFL, FSU 1800 E. Paul Dirac Dr. Tallahassee, FL 32310 Tel: 850-644-6983 [email protected]

Weixing Zhang

St. Jude Children's Research Hospital 262 Danny Thomas Place Memphis, TN 38105 Tel: (901)595-3169 [email protected]

Xu Zhang

Wuhan Institute of Physics and Mathematics Chinese Academy of Sciences Wuhan, 430071 China [email protected]

Yanli Zhang

University of Nebraska Medical Center 986025 Nebraska Medical Center COP3026 Omaha, NE 68198-6025 Tel: 4029960129 [email protected]

Yonghong Zhang

Univ. of Calif,Davis Department of Chemistry University of California, Davis Davis, CA 95616 Tel: 530-754-2036 [email protected]

Zhiyang Zhang

Virginia Polytechnic Inst and State Univ Mail Code 0212, Dept of Chemistry Blacksburg, VA 24060 Tel: 540-231-3571 [email protected]

Ziming Zhang

Sanford-Burnham Medical Research Institute 10901 North Torrey Pines Road La Jolla, CA 92037 Tel: 858-646-3100 [email protected]


Page 150

Donghua H. Zhou Oklahoma State University 230 L HBRC Department of Physics Stillwater, OK 74078 Tel: 405 744-3277 [email protected]

Ronghui Zhou

University of Florida NPB B122 Gainesville, FL 32611 Tel: 3528463114 [email protected]

Xin Zhou

Wuhan Inst. of Physics and Mathematics, CAS 30 West Xiaohongshan Wuhan, Hubei, 430071 China Tel: 87-27-8719-8802 [email protected]

Liu Zhu Wuhan Inst of Physics and Math Xiao Hong Shan West 30, Wuhan 430071, Hubei, PR China Wuhan, Xiao Hong Shan West 30 430071 China Tel: 86 027 87198397 [email protected]

Peizhi Zhu

University of Michigan 930 N.University Ave Ann Arbor, MI 48109 Tel: 734 272 8953 [email protected]

Siqi Zhu

McGill University 801 Sherbrooke St. W. Montreal, QC H2A3K6 Canada [email protected]

Joshua Ziarek

Medical College of Wisconsin 8701 Watertown Plank Road Department of Biochemistry Milwaukee, WI 53226 Tel: 4149552536 [email protected]

Lukas Zidek Masaryk University Kamenice 5 Brno, CZ Brno Czech Republic Tel: 4.2064949839e+011 [email protected]

Kurt Zilm

Yale University Chemistry Department 350 Edwards Street New Haven, CT 06511 Tel: 203 432 3956 [email protected]

Xiaowei Zou

Columbia University 351 Engineering Terrace, Mail Code 8904 1210 Amsterdam Avenue, NY 10027 [email protected]

Nicholas Zumbulyadis

2 Seneca Parkway Rochester, NY 14613 Tel: 585.458.4027 [email protected]

the 53rd enc - enc conference · on behalf of the organizing committee, welcome to the 53rd enc!...

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