The role of dynamics in allosteric regulation

Curr Opin Struct Biol. 2003 Dec;13(6):748-57. doi: 10.1016/j.sbi.2003.10.008.

Abstract

The biomolecular conformational changes often associated with allostery are, by definition, dynamic processes. Recent publications have disclosed the role of pre-existing equilibria of conformational substates in this process. In addition, the role of dynamics as an entropic carrier of free energy of allostery has been investigated. Recent work thus shows that dynamics is pivotal to allostery, and that it constitutes much more than just the move from the 'T'-state to the 'R'-state. Emerging computational studies have described the actual pathways of allosteric change.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Binding Sites
  • Kinetics
  • Models, Chemical
  • Models, Molecular*
  • Motion
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Proteins / chemistry*
  • Stereoisomerism

Substances

  • Proteins