Potential‐energy calculations of terminally blocked tetrapeptides from the third loop of short‐chain snake venom neurotoxins

Abstract

The conformational space of six tetrapeptides from the β‐bends in the third loop of short‐chain snake venom neurotoxins was investigated with the aid of energy calculations. It was shown that these peptides can be divided into two groups: those with a specific preference for an α‐helix and those that exist as an ensemble of β‐turn conformations. © Munksgaard 1994.