  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.
