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• W1886700512 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." @default.
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• W1886700512 date "2015-06-01" @default.
• W1886700512 modified "2023-10-16" @default.
• W1886700512 title "Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions" @default.
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• W1886700512 doi "https://doi.org/10.1016/j.bpj.2015.04.035" @default.
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