Shared Signature Dynamics Tempered by Local Fluctuations Enables Fold Adaptability and Specificity.

ABSTRACT: Recent studies have drawn attention to the evolution of protein dynamics, in addition to sequence and structure, based on the premise structure-encodes-dynamics-encodes-function. Of interest is to understand how functional differentiation is accomplished while maintaining the fold, or how intrinsic dynamics plays out in the evolution of structural variations and functional specificity. We performed a systematic computational analysis of 26,899 proteins belonging to 116 CATH superfamilies. Characterizing cooperative mechanisms and convergent/divergent features that underlie the shared/differentiated dynamics of family members required a methodology that lends itself to efficient analyses of large ensembles of proteins. We therefore introduced, SignDy, an integrated pipeline for evaluating t

SUBMITTER: Zhang S 

PROVIDER: S-EPMC6736388 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature