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Ligand-regulated oligomerisation of allosterically interacting proteins

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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.

Graphical abstract: Ligand-regulated oligomerisation of allosterically interacting proteins

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Publication details

The article was received on 08 May 2018, accepted on 09 Jul 2018 and first published on 10 Jul 2018


Article type: Paper
DOI: 10.1039/C8SM00943K
Citation: Soft Matter, 2018, Advance Article
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    Ligand-regulated oligomerisation of allosterically interacting proteins

    C. Schaefer, R. A. J. de Bruijn and T. C. B. McLeish, Soft Matter, 2018, Advance Article , DOI: 10.1039/C8SM00943K

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