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- W152086352 startingPage "69" @default.
- W152086352 abstract "Formation of high-affinity complexes is critical for the majority of enzymatic reactions involving proteins. The creation of the family of Michaelis and other intermediate complexes during catalysis clearly involves a complicated manifold of interactions that are diverse and complex. Indeed, computing the energetics of interactions between proteins and small molecule ligands using molecular structure alone remains a great challenge. One of the most difficult contributions to the free energy of protein-ligand complexes to access experimentally is that due to changes in protein conformational entropy. Fortunately, recent advances in solution nuclear magnetic resonance (NMR) relaxation methods have enabled the use of measures-of-motion between conformational states of a protein as a proxy for conformational entropy. This review briefly summarizes the experimental approaches currently employed to characterize fast internal motion in proteins, how this information is used to gain insight into conformational entropy, what has been learned, and what the future may hold for this emerging view of protein function." @default.
- W152086352 created "2016-06-24" @default.
- W152086352 creator A5001163598 @default.
- W152086352 creator A5067516774 @default.
- W152086352 creator A5081320421 @default.
- W152086352 date "2013-01-01" @default.
- W152086352 modified "2023-09-26" @default.
- W152086352 title "A Surprising Role for Conformational Entropy in Protein Function" @default.
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