PROTEOMICS, PROTEIN FOLDING AND SELF-ASSOCIATION: NEW INSIGHTS FROM RECENT ADVANCES IN PROTEIN NMR METHDOLOGIES
Nuclear Magnetic Resonance (NMR) spectroscopy has been undergoing unparalleled development, much of which has been driven by applications in structural biology, especially, proteins. We have designed new NMR methods and protocols for rapid chemical shift assignment of protein backbone resonances. These have enabled rapid determination of protein structures, elucidation of folding transitions, and getting valuable insights into protein-protein interaction and self association. These have significant implications for understanding structure-dynamics-function relationships, mechanisms of protein mis-folding, and thus may help in designing of drugs against specific diseases.