Long-range correlation in protein dynamics: Confirmation by structural data and normal mode analysis.

ABSTRACT: Proteins in cellular environments are highly susceptible. Local perturbations to any residue can be sensed by other spatially distal residues in the protein molecule, showing long-range correlations in the native dynamics of proteins. The long-range correlations of proteins contribute to many biological processes such as allostery, catalysis, and transportation. Revealing the structural origin of such long-range correlations is of great significance in understanding the design principle of biologically functional proteins. In this work, based on a large set of globular proteins determined by X-ray crystallography, by conducting normal mode analysis with the elastic network models, we demonstrate that such long-range correlations are encoded in the native topology of the proteins. To unders

SUBMITTER: Tang QY 

PROVIDER: S-EPMC7043781 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature