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Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.

ABSTRACT: There is considerable interest in the dynamic aspect of allosteric action, and in a growing list of proteins allostery has been characterized as being mediated predominantly by a change in dynamics, not a transition in conformation. For considering conformational dynamics, a protein molecule can be simplified into a number of relatively rigid microdomains connected by joints, corresponding to, e.g., communities and edges from a community network analysis. Binding of an allosteric activator strengthens intermicrodomain coupling, thereby quenching fast (e.g., picosecond to nanosecond) local motions but initiating slow (e.g., microsecond to millisecond), cross-microdomain correlated motions that are potentially of functional importance. This scenario explains allosteric effects observed in many unrelated proteins.

SUBMITTER: Guo J

PROVIDER: S-EPMC4472062 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature

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Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.

Guo Jingjing J Zhou Huan-Xiang HX

Biophysical journal 20150601 12

There is considerable interest in the dynamic aspect of allosteric action, and in a growing list of proteins allostery has been characterized as being mediated predominantly by a change in dynamics, not a transition in conformation. For considering conformational dynamics, a protein molecule can be simplified into a number of relatively rigid microdomains connected by joints, corresponding to, e.g., communities and edges from a community network analysis. Binding of an allosteric activator stren ...[more]

PMID: 26083915

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