1H high-resolution magic angle spinning NMR spectroscopy for the investigation of a Ras lipopeptide in a lipid membrane

被引：0
|
作者：
Huster, D
Kuhn, K
Kadereit, D
Waldmann, H
Arnold, K
机构：
[1] Univ Leipzig, Inst Med Phys & Biophys, D-04103 Leipzig, Germany
[2] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2001年 / 40卷 / 06期
关键词：
D O I：
10.1002/1521-3773(20010316)40:6<1056::AID-ANIE10560>3.0.CO;2-7
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A double lipid-modified peptide which mimics the seven amino acids of the C terminus of the N-Ras protein has been investigated by high-resolution 1H magic angle spinning NMR spectroscopy. The axially symmetric motion of the peptide in the bilayer decreases the NMR line widthes, which facilitates signal assignment and localization of the peptide in the membrane (see schematic representation).
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页码：1056 / +
页数：4
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