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J Mol Biol. 2013 May 13;425(9):1410-4. doi: 10.1016/j.jmb.2012.12.008. Epub 2012 Dec 28.

The propagation of allosteric states in large multiprotein complexes.

Author information

1
Department of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DT, UK. db10009@cam.ac.uk

Abstract

A statistical view of allostery leads to a more nuanced and physically realistic picture of protein cooperativity. If the conformational state of one protein molecule in a multiprotein complex influences the probability of a particular conformation in a neighbouring protein, then changes can propagate. Given suitable parameters, linear or two-dimensional arrays of allosteric subunits will then behave similar to an Ising model, exhibiting hypersharp responses to external conditions. Predictions based on this concept find good quantitative agreement in a number of experimental systems including switching of the bacterial flagellar motor, amplification of ligand signals in the Escherichia coli chemotaxis receptors, and termination of calcium sparks in cardiac muscle. A similar mechanism could potentially provide a universal mechanism of integration within living cells.

PMID:
23274139
DOI:
10.1016/j.jmb.2012.12.008
[Indexed for MEDLINE]

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