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Global low-frequency motions in protein allostery : CAP as a model system.

Townsend, P.D. and Rogers, T.L. and Pohl, E. and Wilson, M.R. and McLeish, T.C.B. and Cann, M.J. (2015) 'Global low-frequency motions in protein allostery : CAP as a model system.', Biophysical reviews., 7 (2). pp. 175-182.


Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of Escherichia coli is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.

Item Type:Article
Keywords:Protein, Allostery, Dynamics, Catabolite activator protein, Normal modes, Elastic network model
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Publisher statement:© The Author(s) 2015. This article is published with open access at Open Access. This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
Date accepted:12 January 2015
Date deposited:11 February 2015
Date of first online publication:04 February 2015
Date first made open access:No date available

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