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

ABSTRACT: 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 betw

SUBMITTER: Mitchell MR 

PROVIDER: S-EPMC5056043 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature