Hydration dynamics of the collagen triple helix by NMR

被引:94
作者
Melacini, G
Bonvin, AMJJ
Goodman, M
Boelens, R
Kaptein, R
机构
[1] Univ Utrecht, NMR Dept, Bijvoet Ctr Biomol Res, NL-3508 CH Utrecht, Netherlands
[2] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
关键词
chemical exchange; collagen; hydration; NOE; NMR;
D O I
10.1006/jmbi.2000.3919
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The hydration of the collagen-like Ac-(Gly-Pro-Hyp)(6)-NH2 triple-helical peptide in solution was investigated using an integrated set of high-resolution NMR hydration experiments, including different recently developed exchange-network editing methods. This approach was designed to explore the hydration dynamics in the proximity of labile groups, such as the hydroxyproline hydroxyl group, and revealed that the first shell of hydration in collagen-like triple helices is kinetically labile with upper Limits for water molecule residence times in the nanosecond to sub-nanosecond range. This result is consistent with a "hopping" hydration model in which solvent molecules are exchanged in and out of solvation sites at a rate that is not directly correlated to the degree of site localization. The hopping model thus reconciles the dynamic view of hydration revealed by NMR with the previously suggested partially ordered semi-clathrate-like cylinder of hydration. Ln addition, the nanosecond to sub-nanosecond upper limits for water molecule residence times imply that hydration-dehydration events are not likely to be the rate-limiting step for triple helix self-recognition, complementing previous investigations on water dynamics in collagen fibers. This study has also revealed labile proton features expected to facilitate the characterization of the structure and folding of triple helices in collagen peptides. (C) 2000 Academic Press.
引用
收藏
页码:1041 / 1048
页数:8
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