Topology-dependent entropic differences for chiral polypeptides in solvents

The entropy of topological conformations of helical biopolymers in a solvent is determined as a function of the chirality of winding. Probability distributions are obtained by taking all possible winding conformations of a polypeptide. The results show that between mirror image distributions, there is a difference in entropy arising from a net topological winding number and the interaction of a chiral solute with its environment. This interaction is reflected in a drift coefficient which varies from segment to segment along the length of a biopolymer.