Carbopeptoid Folding:Effects of Stereochemistry,Chain Length,and Solvent

摘要

The folding of a polypeptide chain into the stable three-dimensional structure of a biologically active protein is still not understood in atomic detail.However,several research groups have recently reported successful atomistic simulations of secondary-structure formation,including the formation of helices of different types,beta turns and beta sheets of alpha- and beta-peptides.Insight into the nature of both the folding process and the unfolded state has been obtained from various studies simulating the reversible folding of peptides.This development is encouraging and indicates that the biomolecular force fields in use are approaching the accuracy required to predict folding equilibria,although this has so far been demonstrated only for short polypeptides.