Structural and Entropic Allosteric Signal Transduction Strength via Correlated Motions

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.