Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings.

Citation data:

Proceedings of the National Academy of Sciences of the United States of America, ISSN: 1091-6490, Vol: 113, Issue: 40, Page: E5847-E5855

Publication Year:
2016
Usage 8
Abstract Views 7
Link-outs 1
Captures 36
Readers 36
Social Media 2
Tweets 2
Citations 6
Citation Indexes 6
Repository URL:
http://scholarworks.unist.ac.kr/handle/201301/20644
PMID:
27655887
DOI:
10.1073/pnas.1609462113
PMCID:
PMC5056043
Author(s):
Mitchell, Michael R.; Tlusty, Tsvi; Leibler, Stanislas
Publisher(s):
Proceedings of the National Academy of Sciences; NATL ACAD SCIENCES
Tags:
Multidisciplinary; strain; protein mechanics; protein allostery; elasticity
Most Recent Tweet View All Tweets
article description
In many proteins, especially allosteric proteins that communicate regulatory states from allosteric to active sites, structural deformations are functionally important. To understand these deformations, dynamical experiments are ideal but challenging. Using static structural information, although more limited than dynamical analysis, is much more accessible. Underused for protein analysis, strain is the natural quantity for studying local deformations. We calculate strain tensor fields for proteins deformed by ligands or thermal fluctuations using crystal and NMR structure ensembles. Strains-primarily shears-show deformations around binding sites. These deformations can be induced solely by ligand binding at distant allosteric sites. Shears reveal quasi-2D paths of mechanical coupling between allosteric and active sites that may constitute a widespread mechanism of allostery. We argue that strain-particularly shear-is the most appropriate quantity for analysis of local protein deformations. This analysis can reveal mechanical and biological properties of many proteins.