Spin relaxation enhancement confirms dominance of extended conformations in short alanine peptides

被引：26

作者：

Chen, Kang ^{[1
]}

Liu, Zhigang ^{[2
]}

Zhou, Chunhui ^{[2
]}

Bracken, W. Clay ^{[3
]}

Kallenbach, Neville R. ^{[2
]}

机构：

[1] NIH, NHLBI, Lab Mol Biophys, Bethesda, MD 20892 USA

[2] NYU, Dept Chem, New York, NY 10003 USA

[3] Cornell Univ, Weill Med Coll, Dept Biochem, New York, NY 10021 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 47期

关键词：

intramolecular distances; NMR spectroscopy; pepticles; protein folding;

D O I：

10.1002/anie.200703376

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Local order goes with random coil: An ensemble of peptide structures is generated with over 90% extended conformation for Ala and Pro. The population-averaged long-range distance from the N-terminal spin-label residue (see picture, red dot) to the C-terminal amide proton of Ala (blue dots) is fully consistent with the results from NMR spin relaxation measurements. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

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收藏

页码：9036 / 9039

页数：4

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