Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides

Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides
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DOI:
10.1023/a:1018643312309
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发表时间:
1997-04-01
影响因子:
2.7
通讯作者:
Deese, AJ
Deese, AJ
中科院分区:
生物学3区
文献类型:
--
作者:
Vold, RR;Prosser, RS;Deese, AJ

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为了说明磷脂双胞的效用[Sanders,C.R.和Schwonek,J. P.(1992)Biochemistry,31,8898-8905]作为用于高分辨率NMR研究的膜模拟物,我们记录了十四聚体肽Mastoparan Vespula lewisii在二肉豆蔻酰和二己酰磷脂酰胆碱的各向同性水溶液中的二维H-1 NMR光谱。Mastoparan在水中主要是非结构化的,但呈现与双层相关的明确的螺旋构象。一个明显的周期性的顺序NH化学位移提供了强有力的证据,这短肽的螺旋轴是平行的,而不是垂直的,双层平面。的bicellar的解决方案仍然需要深入的形态表征,但他们似乎是理想的媒体NMR测定的结合模式和膜相关的肽和蛋白质的结构。
In order to illustrate the utility of phospholipid bicelles [Sanders, C.R. and Schwonek, J.P. (1992) Biochemistry, 31, 8898-8905] as a membrane mimetic for high-resolution NMR studies, we have recorded two-dimensional H-1 NMR spectra of the tetradecameric peptide mastoparan Vespula lewisii in an isotropic aqueous solution of dimyristoyl and dihexanoyl phosphatidylcholine. Mastoparan is largely unstructured in water, but assumes a well-defined helical conformation in association with the bilayers. A pronounced periodicity of the sequential NH chemical shifts provides strong evidence that the helix axis of this short peptide is parallel, rather than perpendicular, to the bilayer plane. The bicellar solutions still require in-depth morphological characterization, but they appear to be ideal media for NMR determination of the mode of binding and the structure of membrane-associated peptides and proteins.