Cation-binding location and hydrogen-exchange sites for gramicidin in SDS micelles using NOESY NMR

被引：9

作者：

Hinton, JF

机构：

[1] Department of Chemistry/Biochemistry, University of Arkansas, Fayetteville

来源：

JOURNAL OF MAGNETIC RESONANCE SERIES B | 1996年 / 112卷 / 01期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1006/jmrb.1996.0105

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

The site of monovalent cation binding and sites of hydrogen exchange between amide protons and water molecules in the gramicidin A and Phe-1 gramicidin A channels incorporated into SDS micelles have been determined using a NOESY NMR technique. The cation-binding pocket was found to involve residues 10-15 of the peptide. (C) 1996 Academic Press, Inc.

引用

页码：26 / 31

页数：6

共 26 条

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