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Biophys J. 2006 Sep 15;91(6):2055-62. Epub 2006 Jun 23.

Coupling of global and local vibrational modes in dynamic allostery of proteins.

Author information

1
Interdisciplinary Research Centre in Polymer Science and Technology, School of Physics and Astronomy and Astbury Centre for Structural Biology, University of Leeds, Leeds, United Kingdom.

Abstract

It is now recognized that internal global protein dynamics play an important role in the allosteric function of many proteins. Alterations of protein flexibility on effector binding affect the entropic cost of binding at a distant site. We present a coarse-grained model for a potential amplification of such entropic allostery due to coupling of fast, localized modes to the slow, global modes. We show how such coupling can give rise to large compensating entropic and enthalpic terms. The model corresponds to the pattern of calorimetry and NMR data from experiments on the Met repressor.

PMID:
16798805
PMCID:
PMC1557547
DOI:
10.1529/biophysj.106.082180
[Indexed for MEDLINE]
Free PMC Article

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