Energy minimization studies on cyclic pentapeptide

Abstract

Energy minimization studies have been carried out on an all-trans cyclic pentapeptide (CPP). Various grid search minima have been used as starting points to investigate more thoroughly the conformational variety among cyclic pentapeptides. All the minima possess intramolecular H-bonds, characteristic of β- and γ-turns. Thirteen minima have been picked out, which have distinct schemes of hydrogen bonding and are stereochemically good. These results show that the CPP can adopt multiple structures with β- and γ-turns.