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Allostery without conformation change: modelling protein dynamics at multiple scales

McLeish, Thomas C.B.; Rodgers, T.L.; Wilson, Mark R.

Allostery without conformation change: modelling protein dynamics at multiple scales Thumbnail


Thomas C.B. McLeish

T.L. Rodgers


The original ideas of Cooper and Dryden, that allosteric signalling can be induced between distant binding sites on proteins without any change in mean structural conformation, has proved to be a remarkably prescient insight into the rich structure of protein dynamics. It represents an alternative to the celebrated Monod–Wyman–Changeux mechanism and proposes that modulation of the amplitude of thermal fluctuations around a mean structure, rather than shifts in the structure itself, give rise to allostery in ligand binding. In a complementary approach to experiments on real proteins, here we take a theoretical route to identify the necessary structural components of this mechanism. By reviewing and extending an approach that moves from very coarse-grained to more detailed models, we show that, a fundamental requirement for a body supporting fluctuation-induced allostery is a strongly inhomogeneous elastic modulus. This requirement is reflected in many real proteins, where a good approximation of the elastic structure maps strongly coherent domains onto rigid blocks connected by more flexible interface regions.

Journal Article Type Article
Publication Date Oct 1, 2013
Deposit Date Jun 14, 2014
Publicly Available Date Aug 15, 2014
Journal Physical Biology
Electronic ISSN 1478-3975
Publisher IOP Publishing
Peer Reviewed Peer Reviewed
Volume 10
Issue 5
Public URL


Accepted Journal Article (1.2 Mb)

Copyright Statement
© 2013 IOP Publishing Ltd. This is an author-created, un-copyedited version of an article accepted for publication in Physical Biology. IOP Publishing Ltd is not responsible for any errors or omissions in this version of the manuscript or any version derived from it. The Version of Record is available online at

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