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Updated: Aug 5, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
The 'allosteron' model for entropic allostery of self-assembly
Tom McLeish1, C Schaefer2, A C von der Heydt2
1Department of Physics, Durham University, South Road, Durham DH1 3LE, UK tom.mcleish@york.ac.uk.
Abstract:
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'.
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