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

Jingjing Guo, Huan Xiang Zhou

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2771-2774
Number of pages4
JournalBiophysical Journal
Volume108
Issue number12
DOIs
Publication statusPublished - 18 Jun 2015
Externally publishedYes

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