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Conformational analysis of a 12-residue analogue of mastoparan, a 14-residue peptide from wasp venom

โœ Scribed by C.H. Faerman; D.R. Ripoll


Book ID
103637936
Publisher
Elsevier Science
Year
1992
Tongue
English
Weight
132 KB
Volume
10
Category
Article
ISSN
0263-7855

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Conformational analysis of a 12-residue
โœ Carlos H. Faerman; Daniel R. Ripoll ๐Ÿ“‚ Article ๐Ÿ“… 1992 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 542 KB

## Abstract 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 us

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Recent studies have shown that mastoparan, an amphiphilic peptide derived from wasp venom, modifies the secretion of neurotransmitters and hormones from a variety of cell types. Mastoparan interacts with heterotrimeric guanine nucleotide-binding proteins (G proteins) such as Gi and G(o), which are A