Entropy Transfer and Dynamics of Allostery in Proteins

TL;DR

This paper introduces a master equation model of protein allostery based on entropy transfer, linking conformational dynamics to functional communication within proteins.

Contribution

It presents a novel theoretical framework connecting entropy transfer to allosteric signaling in proteins using a master equation approach.

Findings

Entropy transfer models asymmetric information flow in proteins

The model relates conformational transitions to entropy transfer dynamics

Insights into how allostery influences protein function

Abstract

Allostery is an intrinsic spatiotemporal property of all proteins, resulting from long range correlations in the order of several nanometers and time scales of nanoseconds. Information is carried asymmetrically from one part to another by entropy transfer. Here, we present a master equation model of allosteric communication in proteins based on the transfer entropy concept of Schreiber (PRL, 85, 465, 2000). We show how the model relates the path and velocity of asymmetric entropy transfer to conformational transitions over the rugged energy surface of proteins and how this relates to function.