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Applications of NMR and computational methodologies to study protein dynamics

Author:
Chitra Narayanan  Khushboo Bafna  Louise D. Roux  Pratul K. Agarwal  Nicolas Doucet  


Journal:
Archives of Biochemistry and Biophysics


Issue Date:
2017


Abstract(summary):

Abstract Overwhelming evidence now illustrates the defining role of atomic-scale protein flexibility in biological events such as allostery, cell signaling, and enzyme catalysis. Over the years, spin relaxation nuclear magnetic resonance (NMR) has provided significant insights on the structural motions occurring on multiple time frames over the course of a protein life span. The present review article aims to illustrate to the broader community how this technique continues to shape many areas of protein science and engineering, in addition to being an indispensable tool for studying atomic-scale motions and functional characterization. Continuing developments in underlying NMR technology alongside software and hardware developments for complementary computational approaches now enable methodologies to routinely provide spatial directionality and structural representations traditionally harder to achieve solely using NMR spectroscopy. In addition to its well-established role in structural elucidation, we present recent examples that illustrate the combined power of selective isotope labeling, relaxation dispersion experiments, chemical shift analyses, and computational approaches for the characterization of conformational sub-states in proteins and enzymes. Graphical abstract Image 1 Highlights • Atomic flexibility on multiple time scales plays a defining role in protein function. • NMR relaxation allows the characterization of protein conformational sub-states. • Computational and biophysical applications further expand the range of NMR methods. • This review presents recent application progress to a general biochemical audience.


Page:
71-71


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