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掺入十二烷基硫酸钠胶束中的甘氨酸-11短杆菌肽A的物种异质性。

Species heterogeneity of Gly-11 gramicidin A incorporated into sodium dodecyl sulfate micelles.

作者信息

Hinton J F, Washburn A M

机构信息

Department of Chemistry/Biochemistry, University of Arkansas, Fayetteville 72701, USA.

出版信息

Biophys J. 1995 Aug;69(2):435-8. doi: 10.1016/S0006-3495(95)79916-7.

Abstract

Evidence is presented for species heterogeneity of the gly-11 analog of gramicidin A incorporated into sodium dodecyl sulfate (SDS) micelles. The evidence for species heterogeneity has been obtained using one-dimensional (1D) 1H NMR spectroscopy. The 1D spectra of the indole NH moiety of tryptophans 9, 13, and 15 show the presence of more than one species. It has been found that the heterogeneity is dependent upon the gly-11/SDS molar ratio. At high SDS concentration (i.e., gly-11/SDS of 3 mM/700 mM) the heterogeneity almost completely disappears. The temperature dependence of these 1H NMR signals suggests that the two species do not interconvert. The results of nuclear Overhauser effect spectroscopy NMR experiments indicate that one species is embedded within the micelle, while the other is nearer the aqueous interface. The importance of side chain interactions with the membrane environment in producing stable, solubilized species of small peptides in SDS micelles is illustrated.

摘要

本文提供了关于掺入十二烷基硫酸钠(SDS)胶束中的短杆菌肽A的gly - 11类似物的物种异质性的证据。物种异质性的证据是通过一维(1D)1H NMR光谱获得的。色氨酸9、13和15的吲哚NH部分的1D光谱显示存在不止一种物种。已发现异质性取决于gly - 11/SDS摩尔比。在高SDS浓度下(即gly - 11/SDS为3 mM/700 mM),异质性几乎完全消失。这些1H NMR信号的温度依赖性表明这两种物种不会相互转化。核Overhauser效应光谱NMR实验结果表明,一种物种嵌入胶束内,而另一种更靠近水相界面。说明了侧链与膜环境的相互作用在SDS胶束中产生稳定的、可溶解的小肽物种方面的重要性。

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本文引用的文献

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Membrane protein conformational change dependent on the hydrophobic environment.
Biochemistry. 1985 Apr 9;24(8):1920-8. doi: 10.1021/bi00329a018.

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