Ontology highlight
ABSTRACT:
SUBMITTER: McLeish T
PROVIDER: S-EPMC5941180 | biostudies-literature | 2018 Jun
REPOSITORIES: biostudies-literature
McLeish Tom T Schaefer C C von der Heydt A C AC
Philosophical transactions of the Royal Society of London. Series B, Biological sciences 20180601 1749
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) <i>n</i>-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 ...[more]