| Literature DB >> 3338566 |
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.Entities:
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Year: 1988 PMID: 3338566 DOI: 10.1016/0014-5793(88)81405-4
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124