Resonance

, Volume 22, Issue 1, pp 37–50 | Cite as

Allosteric regulation of proteins

A historical perspective on the development of concepts and techniques
General Article
First Online:

Abstract

Allostery is a mechanism by which the activity of a large number of proteins is regulated. It is manifested as a change in the activity, either ligand binding or catalysis of one site of a protein due to a ligand binding to another distinct site of the protein. The allosteric effect is transduced by a change in the structural properties of the protein. It has been traditionally understood using either the concerted MWC (Monod, Wyman and Changeux) model, or the sequential KNF (Koshland, Nemethy and Filmer) model of structural changes. However, allostery is fundamentally a thermodynamic process and requires an alteration in the enthalpy or entropy associated with the process.

Keywords

Proteins allostery regulation enthalpy entropy 
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Copyright information

© Indian Academy of Sciences 2017

Authors and Affiliations

  1. 1.Department of Molecular Reproduction Development and Genetics Biology Building GA09Indian Institute of ScienceBengaluruIndia

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