Ligand-regulated oligomerisation of allosterically interacting proteins

Charley Schaefer; René A.J. De Bruijn; Tom C.B. McLeish

doi:10.1039/c8sm00943k

Ligand-regulated oligomerisation of allosterically interacting proteins

Charley Schaefer^*, René A.J. De Bruijn, Tom C.B. McLeish

^*Corresponding author for this work

Physics

Research output: Contribution to journal › Article › peer-review

Abstract

The binding of ligands to distinct sites at proteins or at protein clusters is often cooperative or anti-cooperative due to allosteric signalling between those sites. The allostery is usually attributed to a configurational change of the proteins from a relaxed to a configurationally different tense state. Alternatively, as originally proposed by Cooper and Dryden, a tense state may be achieved by merely restricting the thermal vibrations of the protein around its mean configuration. In this work, we provide theoretical tools to investigate fluctuation allostery using cooling and titration experiments in which ligands regulate dimerisation, or ring or chain formation. We discuss in detail how ligands may regulate the supramolecular (co)polymerisation of liganded and unliganded proteins.

Original language	English
Pages (from-to)	6961-6968
Number of pages	8
Journal	Soft Matter
Volume	14
Issue number	34
DOIs	https://doi.org/10.1039/c8sm00943k
Publication status	Published - 10 Jul 2018

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© The Royal Society of Chemistry 2018. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

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© The Royal Society of Chemistry 2018. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.
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Cite this

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Ligand-regulated oligomerisation of allosterically interacting proteins

Abstract

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