A two‐dimensional NMR study of the antimicrobial peptide magainin 2

FEBS Letters

Bax, Ad¹  Zasloff, Michael²  Marion, Dominique¹ 

[1] Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA;Human Genetics Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Peptide;    α-Helix;    Magainin;    2D NMR;    NOESY;    2D;    two-dimensional;    NOE;    nuclear Overhauser effect;    NOESY;    NOE spectroscopy;    HOHAHA;    homonuclear Hartmann-Hahn spectroscopy;    TFE;    trifluoroethanol;   

DOI  :  10.1016/0014-5793(88)81405-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown