期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 132, 期 14, 页码 5015-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja100645k
关键词
-
资金
- DFG [Re1435]
- NSF [CHE-0723718]
Analyses of solution N-15 relaxation data and solid-state H-1(N)-N-15 dipolar couplings from a small globular protein, alpha-spectrin SH3 domain, produce a surprisingly similar pattern of order parameters. This result suggests that there is little or no ns-mu s dynamics throughout most of the sequence and, in particular, in the structured portion of the backbone. At the same time, evidence of ns-mu s motions is found in the flexible loops and termini. These findings, corroborated by the MD simulations of alpha-spectrin SH3 in a hydrated crystalline environment and in solution, are consistent with the picture of protein dynamics that has recently emerged from the solution studies employing residual dipolar couplings.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据