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Review
. 2011 Feb;21(1):62-7.
doi: 10.1016/j.sbi.2010.10.007. Epub 2010 Nov 23.

Protein dynamics and allostery: an NMR view

Shiou-Ru Tzeng  1 , Charalampos G Kalodimos
Affiliations
Review

Protein dynamics and allostery: an NMR view

Shiou-Ru Tzeng et al. Curr Opin Struct Biol. 2011 Feb.

Abstract

Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link between internal motions over a wide range of time scales and function in protein-ligand interactions. Proteins respond to perturbations by redistributing their motions and they use fluctuating conformational states for binding and conformational entropy as a carrier of allosteric energy to modulate association with ligands. In several cases allosteric interactions proceed with minimal or no structural changes. We discuss emerging paradigms for the central role of protein dynamics in allostery.

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