Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study.
Molecular dynamics of collagen side chains in hard and soft tissues. A multinuclear magnetic resonance study.
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硬组织和软组织中胶原蛋白侧链的分子动力学。
DOI：
10.1021/bi00395a032
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发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Torchia,DA
中科院分区：
文献类型：
--
作者：
Sarkar,SK;Hiyama,Y;Niu,CH;Young,PE;Gerig,JT;Torchia,DA
We have prepared samples of (a) intact calvaria collagen (cross-linked and mineralized),(b) intact tendon collagen (cross-linked but not mineralized), and (c) reconstituted chick calvaria collagen (not cross-linked and not mineralized) containing [methyl-2H3] methionyl,[4, 4-2H2] pyrrolidinyl,(4-fluorophenyl) alanyl, and [6-15N] lysyl residues. Using multinuclear magnetic resonance spectroscopy, we have investigated the molecular dynamics of the labeled amino acids. Guided by model compound studies, we reached the following conclusions regarding collagen side chain dynamics from our analysis of line shapes and relaxation rates. At 22 C, imino residues in all samples have flexible rings with root mean square angular fluctuations in the 11-30 range. Nearly all labeled amino acid side chains reorient about at least two side chain single bonds. At temperatures below-30 C, most of these side chain motions are absent in all the samples. Surprisingly, in contrast with results obtained for backbone motions, side chain motions are only marginally more hindered in mineralized samples as compared with nonmineralized samples, a result we discuss with reference to collagen-mineral interactions. We also discuss the possible relationship between collagen dynamics and function.Recently, multinuclear solid-state nuclear magnetic resonance (NMR) 1 spectroscopy was used to compare the mo-lecular dynamics of the collagen backbone in three types of collagen fibers:(a) in reconstituted fibers of chickcalvaria collagen that are not cross-linked and not mineralized;(b) in intact rat tail tendon collagen fibers that are cross-linked but not mineralized;(c) inintact rat calvaria collagen fibers that
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影响因子：
5.6
作者：
BONAR, LC;LEES, S;MOOK, HA
通讯作者：
MOOK, HA
影响因子：
4
作者：
FRASER, RDB;TRUS, BL
通讯作者：
TRUS, BL
胶原分子结构和动力学的多核磁共振研究
影响因子：
2.9
作者：
D. Torchia;Y. Hiyama;S. Sarkar;C. Sullivan;P. Young
通讯作者：
P. Young
原纤维和溶液中胶原骨架运动的 13C/1H 高功率双磁共振研究。
影响因子：
5.6
作者：
L. Jelinski;D. Torchia
通讯作者：
D. Torchia
整合膜蛋白细菌视紫红质的表面动力学
影响因子：
64.8
作者：
M. Keniry;H. S. Gutowsky;E. Oldfield
通讯作者：
E. Oldfield