It has been suggested that the stability of a beta-peptide helical fold is affected by the interplay between the electrical charge of terminal groups and the dipole due to the helical conformation, the so-called charge-dipole stabilization; the numerical simulations presented herein test that suggestion. The motions of two beta-peptide oligomers, each of which has been shown by NMR spectroscopy to fold into a different helical conformation, have been simulated. The simulated motions bear out empirical observations as to the effect of chemical protection of terminal groups on the stability of beta-peptide helical folds and they support the hypothesis of charge-dipole stabilization.
2006 Wiley-Liss, Inc.