Conformational analysis of a 12-residue analogue of mastoparan and of mastoparan X.
We have investigated the conformational properties of a truncated analogue of mastoparan and of mastoparan X, both peptides from wasp venom. The electrostatically driven Monte Carlo method was used to explore the conformational space of these short peptides. The initial conformations used in this study, mainly random ones, led to alpha-helical conformations. The alpha-helical conformations thus found exhibit an amphipathic character. These results are in accord with experimental data from NMR and CD spectroscopy.
Faerman
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Protein Engineering Section, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.
Ripoll
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D000595:Amino Acid Sequence; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D009842:Oligopeptides / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013057:Spectrum Analysis; D014862:Wasp Venoms / Q000737:chemistry*
D036341:Intercellular Signaling Peptides and Proteins; D009842:Oligopeptides; D010455:Peptides; D014862:Wasp Venoms; C075086:mastoparan, des-Ile(1)-des-Asn(2)-; C037500:mastoparan; C071123:mastoparan X