Backbone dynamics in collagen

被引：8

作者：

Aliev, AE ^{[1
]}

机构：

[1] UCL, Dept Chem, Christopher Ingold Labs, London WC1H 0AJ, England

来源：

CHEMICAL PHYSICS LETTERS | 2004年 / 398卷 / 4-6期

关键词：

D O I：

10.1016/j.cplett.2004.09.114

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Peptide backbone motions of collagen have been extensively studied in the past. The experimental results were interpreted using a model of a collagen rod librating about its helix axis. Considering the size of the collagen molecule and the presence of cross-linked molecules, motional amplitudes derived for the helix axis libration were unusually high. Using solid-state NMR C-13 chemical shift anisotropy and H-2 quadrupolar lineshape analysis for five different isotope labelled collagens we show that motional averaging of the NMR interactions occurs primarily via small-angle librations about internal bond directions. This type of dynamics is compatible with both the presence of cross-links in collagen and the X-ray data, as well as dynamic models used for other proteins. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：522 / 525

页数：4

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