Potential-energy calculations of terminally blocked tetrapeptides from the third loop of short-chain snake venom neurotoxins.
The conformational space of six tetrapeptides from the beta-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 alpha-helix and those that exist as an ensemble of beta-turn conformations.
Roos
H M
HM
Department of Chemistry, University of Pretoria, South Africa.
van Rooyen
P H
PH
D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D012910:Snake Venoms / Q000737:chemistry*; D013816:Thermodynamics
D009498:Neurotoxins; D010455:Peptides; D012910:Snake Venoms