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’.
Funder
Engineering and Physical Sciences Research Council
Subject
General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology
Cited by
16 articles.
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