Studying the Stability of a Helical β‐Heptapeptide by Molecular Dynamics Simulations

β‐Peptides consisting entirely of homochiral β‐amino acids R‐CH(NH 2 )‐CH 2 CO 2 H form 3 1 ‐helices in solution, as shown previously by NMR analysis of pyridine and methanol solutions. The stability of the helical secondary structure of one such β‐peptide (H‐β‐HVal‐β‐HAla‐β‐HLeu‐( S,S )‐β‐HAla(αMe)‐β‐HVal‐β‐HAla‐β‐HLeu‐OH, 1 ) has been investigated by molecular dynamics simulations using the GROMOS 96 molecular model and force field (962 methanol molecules; T = 298, 350, 400 K; with and without NOE distance restraints). The restraints derived from the NMR studies were equally well satisfied by both the restrained and the unrestrained room‐temperature molecular dynamics simulations. The 3 1 ‐helical conformation of 1 was shown to be so stable that it was restored spontaneously within 400 ps after unfolding had been induced by a sudden increase of the temperature from 298 to 350 K.