Conformation of the Helix—Coil—Helix Polypeptide

Semi-empirical energy calculations were performed to determine the conformation of the α-helix—random coil—α-helix polypeptide. The random-coil region includes only one amino acid residue in these calculations. The results are illustrated by conformational energy maps. The results indicate that the conformation of the structures is not uniquely determined, but the dihedral angles of the residue in the random region are significantly restricted.