gpcr edition – week 1

GPCR Edition – Week 1

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Amino Acid

Structure

Amino Acids: Misc.

GPCR Structure

Chemical Interactio

ns

Protein Secondary & Tertiary Structure

Potpourri

GLYCINE

VALINE

CYSTEINE

Histidine

TRYPTOPHAN

THE AMINO ACID ARGININE HAS THIS

GROUPING OF AMINO ACIDS, ALONG WITH

LYCINE AND HISTIDINE (IF THE PH IS JUST

RIGHT)POSITIVELY CHARGED

THIS AMINO ACID CAN BE ABBREVIATED AS

“GLN” OR “Q”

GLUTAMINE

THE AMINO ACID ARGININE IS

ABBREVIATED AS “ARG” AS WELL AS THIS ONE LETTER

R

“ALPHA” REFERS TO THIS ELEMENT THAT IS COVALENTLY BONDED TO AN AMINO GROUP, A CARBOXYL GROUP, A

HYDROGEN, AND A SIDE CHAIN

CARBON

THIS NUMBER IS THE NET NEGATIVE OR

POSITIVE CHARGE OF THE FOLLOWING

SHORT OLIGOPEPTIDE:DEKHR

+1

GPCRS ARE ALSO KNOWN AS

HETPAHELICAL RECEPTORS, MEANING

THEY HAVE THIS NUMBER OF ALPHA

HELICESSEVEN

PHOSPHOLIPID

GPCRS ARE EMBEDDED INTO A

MEMBRANE BILAYER COMPOSED OF THIS TYPE OF BIOLOGICAL

MOLECULE

GPCRS ARE VERY DIFFICULT TO

CRYSTALLIZE AND OFTEN TIMES HAVE

CRYSTALLIZATION “HANDLES” FUSED TO

THEM. THIS ONE IS SIMILAR TO WHAT WE

USED IN OUR EXPERIMENT.T4 LYSOZYME

THIS CLASS OF GPCRS HAS A LARGE

EXTRACELLULAR DOMAIN WITH A

“VENUS-FLYTRAP” STRUCTURE WHERE

LIGANDS BINDCLASS C

CLASS A GPCRS HAVE THIS CONSERVED

SEQUENCE MOTIF OF THREE AMINO ACIDS

THAT MEDIATES COUPLING TO G

PROTEINSDRY, ASP-ARG-TYR

THE ATTRACTION OF A CATION TO AN ANION IS REFERRED TO AS THIS

TYPE OF NON-COVALENT CHEMICAL

INTERACTIONIONIC/

ELECTROSTATIC

HYDROGEN BOND

THE NON-COVALENT INTERACTION SHOWN

HERE

THIS NON-COVALENT IS WHAT DRIVES NON-POLAR AMINO ACIDS

TO ORIENT THEMSELVES

TOWARDS THE INTERIOR OF A

PROTEIN AND AWAY FROM WATERHYDROPHOBIC

EFFECT

CARBOXYL

A PEPTIDE BOND IS A COVALENT CHEMICAL

INTERACTION BETWEEN THE AMINO GROUP OF ONE AMINO ACID AND THIS GROUP

OF THE OTHER

HYDROGEN BONDING BETWEEN THE CARBONYL

OXYGEN AND AMINO GROUP HYDROGEN OF TWO AMINO ACIDS 4 RESIDUES APART STABILIZES THIS TYPE OF

STRUCTUREALPHA HELIX

DAILY DOUBLE

THIS IS THE SIMPLEST ARRANGEMENT A

POLYPEPTIDE CHAIN CAN MAKE IN TERMS

OF SECONDARY STRUCTURE

ALPHA HELIX

THIS AMINO ACID’S RIGIDITY RESULTS IN ITS LOW PROBABILITY OF BEING FOUND IN

AN ALPHA HELIX

PROLINE

THE PARTIAL POSITIVE AND NEGATIVE CHARGE OF AN ALPHA HELIX N- AND C-

TERMINUS, RESPECTIVELY, IS REFERRED TO AS THIS

HELIX DIPOLE

THIS IS THE NAME OF THE CHART THAT MEASURES THE PROBABILITY OF

PARTICULAR PSI AND PHI ANGLES TO BE

FOUND IN SECONDARY STRUCTURERAMACHANDRAN

THIS PROTEIN STRUCTURAL MOTIF IS

NAMED AFTER A COMMON

ARCHITECTURAL DESIGN FOUND IN THE

HELLENIC REPUBLICGREEK KEY MOTIF

THIS LEVEL OF PROTEIN STRUCTURE IS THE

ARRANGEMENT OF 2 OR MORE SEPARATE

POLYPEPTIDE CHAINS (SUBUNITS)

QUATERNARY

GPCRS ARE COMPOSED PRIMARILY

OF THIS TYPE OF SECONDARY STRUCTURE

ALPHA HELIX

THE FUNCTIONAL AND FOLDED STRUCTURE OF A PROTEIN IN ITS

NORMAL ENVIRONMENT IS KNOWN AS THIS

NATIVE CONFORMATION

THE FORMATION OF A PEPTIDE BOND BETWEEN

TWO AMINO ACIDS RESULTS IN THE

CREATION OF THIS MOLECULE, WHICH IS WHY THE REACTION IS

CALLED CONDENSATIONWATER

WHICH UNIVERSITY IS THE ONLY ONE IN NCAA HISTORY TO

HOLD THE NATIONAL TITLE IN BOTH

BASKETBALL AND FOOTBALL?

UNIVERSITY OF FLORIDA