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Ligand-regulated oligomerisation of allosterically interacting proteins

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JournalSoft Matter
DateAccepted/In press - 9 Jul 2018
DatePublished (current) - 10 Jul 2018
Issue number34
Volume14
Number of pages8
Pages (from-to)6961-6968
Original languageEnglish

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.

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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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