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

TY - JOUR

T1 - The ‘allosteron’ model for entropic allostery of self-assembly

AU - McLeish, Tom

AU - Schaefer, C.

AU - von der Heydt, A. C.

N1 - © 2018 The Author(s)

PY - 2018/6/19

Y1 - 2018/6/19

N2 - 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’.

AB - 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’.

KW - Allostery

KW - Ligand-binding

KW - Self-assembly

UR - http://www.scopus.com/inward/record.url?scp=85046768435&partnerID=8YFLogxK

U2 - 10.1098/rstb.2017.0186

DO - 10.1098/rstb.2017.0186

M3 - Article

AN - SCOPUS:85046768435

SN - 0962-8436

VL - 373

JO - Philosophical Transactions of the Royal Society B: Biological Sciences

JF - Philosophical Transactions of the Royal Society B: Biological Sciences

IS - 1749

M1 - 20170186

ER -