REVERSIBLE PEPTIDE FOLDING IN SOLUTION BY MOLECULAR-DYNAMICS SIMULATION

Long-standing questions on how peptides fold are addressed by the simu lation at different temperatures of the reversible folding of a peptid e in solution in atomic detail. Molecular dynamics simulations correct ly predict the structure that is thermodynamically stable at 298 K, ir respective of the initial peptide conformation. The rate of folding an d the free energy of folding at different temperatures are estimated. Although the conformational space potentially accessible to the peptid e is extremely large, very few conformers (10(1) to 10(2)) are signifi cantly populated at 20 K above the melting temperature. This implies t hat the search problem in peptide (or even protein) folding is surmoun table using dynamics simulations. (C) 1998 Academic Press.