Abstract
Using two-dimensional NMR spectroscopy, a complete 1H resonance assignment has been obtained for the peptide magainin 2 recently isolated from Xenopus laevis. It is demonstrated that this peptide adopts an alpha-helical structure with amphiphilic character when dissolved in a mixture of trifluoroethanol (TFE) and H2O. The transition to the alpha-helical conformation occurs at very low concentrations of TFE.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Anti-Infective Agents
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Antimicrobial Cationic Peptides*
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Magainins
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Magnetic Resonance Spectroscopy
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Peptides*
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Protein Conformation
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Solutions
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Trifluoroethanol / pharmacology
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Water
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Xenopus Proteins*
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Xenopus laevis
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Magainins
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Peptides
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Solutions
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Xenopus Proteins
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Water
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magainin 2 peptide, Xenopus
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Trifluoroethanol