Proline-induced kink in a helix arises primarily from dihedral angle energy: a molecular dynamics simulation on alamethicin

To investigate the cause of the kink in a helix induced by proline, a restrained molecular dynamics simulation was performed on alamethicin (Alm), a channel-forming peptide. Results on the linear and kinked helices indicated that the kinked form has lower energy than the linear one and the difference can be attributed largely to the dihedral angle term. The argument is strengthened by calculated results on the peptide in which proline 14 was substituted by alanine. The kinked and linear forms had virtually the same total and dihedral angle energies for the alanine analog. Possible implications for Aim voltage-gating are discussed. (C) 1999 Elsevier Science B.V. All rights reserved.