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• W2313615156 startingPage "1722" @default.
• W2313615156 abstract "Allosteric signal transduction in biomacromolecules can play an essential role in their function. Internal motional correlations in proteins provide a possible communication mechanism, but the quantitative relationship between statistical correlations and allostery is unknown. Quantitative relationships between internal motional correlations and the efficiency of propagation of allosteric structural and entropic effects are introduced and validated against conformational ensembles obtained from molecular dynamics simulations. This framework can explain a range of phenomena, such as the occurrence of an allosteric entropy change in the absence of any noticeable structural change." @default.
• W2313615156 created "2016-06-24" @default.
• W2313615156 creator A5083330988 @default.
• W2313615156 creator A5083494373 @default.
• W2313615156 date "2012-06-12" @default.
• W2313615156 modified "2023-09-27" @default.
• W2313615156 title "Structural and Entropic Allosteric Signal Transduction Strength via Correlated Motions" @default.
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• W2313615156 doi "https://doi.org/10.1021/jz300488e" @default.
• W2313615156 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26285736" @default.
• W2313615156 hasPublicationYear "2012" @default.
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