Course Identification

Course for Chemistry and Life Sciences Students. The aim of the course is to give an overview of the applications of NMR for studying protein structure and dynamics, and for characterizing protein-ligand and protein-protein interactions in biological systems. Topics to be covered: multi dimensional NMR techniques, triple-resonance sequential assignment of proteins, secondary structure and 3D structure calculation, PRE, PCS,  chemical exchange and protein-ligand interaction, protein dynamics to study invisible states by NMR.
 

Upon successful completion of this course students should be able to:

1.Critically read and review current literature which describes the use of NMR for structural and dynamics studies of proteins and their interactions with ligands.

2.Understand the capabilities and limitations of NMR in the study of biological systems.

NMR of Protein and Nucleic Acids/   Kurt Wuthrich

NMR of Macromolecules: A Practical Approach/  G.C.K. Roberts, Editor

An NMR Primer for Life Scientists/   Henry Rattle

Biomolecular NMR Spectroscopy/   Jeremy N.S. Evans

Protein NMR Techniques, Methods in Molecular Biology Vol 60/  David G. Reid., Editor  (https://link-springer-com.ezproxy.weizmann.ac.il/book/10.1385%2F0896033090 )

Structural Biology: Practical NMR Application/  Quincy Teng

NMR Primer: An HSQC-based Approach/  Steven M. Pascal

Protein NMR Spectroscopy: Principles and Practice (2nd edition)/ Cavanagh J., Fairbrother W.J., Palmer A.G. III, Skelton N.J.