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The ‘allosteron’ model for entropic allostery of self-assembly

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Publication details

JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
DateAccepted/In press - 15 Feb 2018
DateE-pub ahead of print - 7 May 2018
DatePublished (current) - 19 Jun 2018
Issue number1749
Number of pages8
Early online date7/05/18
Original languageEnglish


Using the simple ‘allosteron’ model, we show that it is possible, in principle, to elicit pathways by which fluctuation allostery affects self-assembly of protein complexes. We treat the cases of (i) protein fibrils and nucleation, (ii) n-mer protein complexes, and (iii) weakly attractive allosteric interactions in protein-like soft nanoscale objects that can be tuned to define exclusive self-associating families. This article is part of a discussion meeting issue ‘Allostery and molecular machines’.

Bibliographical note

© 2018 The Author(s)

    Research areas

  • Allostery, Ligand-binding, Self-assembly

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