Journal
PHYSICAL BIOLOGY
Volume 10, Issue 5, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/1478-3975/10/5/056004
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Funding
- EPSRC [EP/H051759/1]
- EPSRC [EP/H051759/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/H051759/1] Funding Source: researchfish
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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.
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