Chem518 A Fast Introduction/Review of Biological NMR Spectroscopy Introduction to NMR Spectroscopy Nuclear Spin CW NMR Chemical shift, J coupling, intensity Pulsed Fourier Transform (FT) NMR FID, T1, T2, linewidth NMR of the Amino Acids Amino acid spectra Solvents and hydrogen exchange Solvent suppression pKa measurements An Introduction to Protein NMR NMR of peptides and proteins Structure induced chemical shift changes Monitoring protein folding (a co-operative 2 state transition) 2D-NMR Spectroscopy Correlations The COSY experiment COSY spectra of amino acids Sequential Assignment of the NMR Spectra of Proteins Spin systems from COSY-type spectra (through bonds) The Nuclear Overhauser Effect (NOE). Sequential connections from NOESY spectra (through space) The Determination of the Secondary Structures of Proteins NOE patterns for a-helices, b-sheets, and turns J coupling patterns Hydrogen bonding and hydrogen exchange Chemical shifts The Determination of the Tertiary Structures of Proteins Distances from the NOESY experiment Model Building Distance Geometry Molecular Dynamics Representing the 3D structures of proteins A Comparison to X-Ray Crystallography A basic comparison (conditions, limitations, structure quality) Protein structures in solution vs. a crystal Incorrect structures Introduction to Protein Dynamics Protein motions Aromatic ring flipping Amide hydrogen exchange