A two‐dimensional NMR study of the antimicrobial peptide magainin 2
- 18 January 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 227 (1), 21-26
- https://doi.org/10.1016/0014-5793(88)81405-4
Abstract
Using two-dimensional NMR spectroscopy, a complete 1H resonance assignment has been obtained for the peptide magaining 2 recently isolated from Xenopus laevis. It is demonstrated that this peptide adopts an α-helical structure with amphiphilic character when dissolved in a mixture of trifluoroethanol (TFE) and H2O. The transition to the α-helical conformation occurs at very low concentrations of TFE.Keywords
This publication has 12 references indexed in Scilit:
- Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.Proceedings of the National Academy of Sciences, 1987
- PEPTIDES WITH AFFINITY FOR MEMBRANESAnnual Review of Biophysics, 1987
- Solution structure of human growth hormone releasing factorJournal of Molecular Biology, 1986
- MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopyJournal of Magnetic Resonance (1969), 1985
- THREE-DIMENSIONAL STRUCTURE OF MEMBRANE AND SURFACE PROTEINSAnnual Review of Biochemistry, 1984
- Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonanceJournal of Molecular Biology, 1983
- Coherence transfer by isotropic mixing: Application to proton correlation spectroscopyJournal of Magnetic Resonance (1969), 1983
- A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrantsJournal of Magnetic Resonance (1969), 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Active polypeptides: from amphibian skin to gastrointestinal tract and brain of mammalsTrends in Pharmacological Sciences, 1980