A TWO-DIMENSIONAL NMR-STUDY OF THE ANTIMICROBIAL PEPTIDE MAGAININ-2
A TWO-DIMENSIONAL NMR-STUDY OF THE ANTIMICROBIAL PEPTIDE MAGAININ-2
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DOI：
10.1016/0014-5793(88)81405-4
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发表时间：
1988-01-18
期刊：
影响因子：
3.5
通讯作者：
BAX, A
中科院分区：
文献类型：
--
作者：
MARION, D;ZASLOFF, M;BAX, A
利用二维核磁共振波谱技术，对最近从非洲爪蟾（xenopus laevis）中分离到的肽magainm2进行了完整的1h共振分配。结果表明，该肽在三氟乙醇（TFE）和水的混合物中溶解时呈α-螺旋结构，具有两亲性。向α-螺旋构象的转变发生在极低浓度的TFE中。
Using two-dimensional NMR spectroscopy, a complete1H resonance assignment has been obtained for the peptide magaining 2 recently isolated fromXenopus 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.