Probing side-chain dynamics in proteins by the measurement of nine deuterium relaxation rates per methyl group

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	Probing side-chain dynamics in proteins by the measurement of nine deuterium relaxation rates per methyl group
	Liao, Xinl ; Long, Dong ; Li, Da-Wei ; Br眉schweiler, Rafael ; Tugarinov, Vitali ; Liao XL(廖新丽)
刊名	http://dx.doi.org/10.1021/jp209304c
	2012
关键词	Deuterium Dynamics Functional groups Inverse kinematics Molecular dynamics Spin dynamics
英文摘要	We demonstrate the feasibility of the measurement of up to nine deuterium spin relaxation rates in 13CHD2 and 13CH 2D methyl isotopomers of small proteins. In addition to five measurable 2H relaxation rates in a 13CH2D methyl group (Millet, O.; Muhandiram, D. R.; Skrynnikov, N. R.; Kay, L. E.J. Am. Chem. Soc. 2002, 124, 6439-48), the measurement of additional four rates of (nearly) single-exponentially decaying magnetization terms in methyl groups of the 13CHD2 variety is reported. Consistency relationships between 2H spin relaxation rates measured in the two different types of methyl groups are derived and verified experimentally for a subset of methyl-containing side chains in the protein ubiquitin. A detailed comparison of methyl-bearing side-chain dynamics parameters obtained from relaxation measurements in 13CH2D and 13CHD2 methyls of ubiquitin at 10, 27, and 40 掳C reveals that transverse 2H relaxation rates in 13CHD2 groups are reliable and accurate reporters of the amplitudes of methyl 3-fold axis motions (Saxis2) for protein molecules with global molecular tumbling times 蟿C > 鈭? ns. For smaller molecules, simple correction of transverse 2H relaxation rates in 13CHD2 groups is sufficient for the derivation of robust measures of order. Residue-specific distributions of Saxis2 are consistent with atomic-detail molecular dynamics (MD) results. Both 13CHD2- and 13CH 2D-derived Saxis2 values are in good overall agreement with those obtained from 1 渭s MD simulations at all the three temperatures, although some differences in the site-specific temperature dependence between MD- and 2H-relaxation-derived Saxis2 values are observed. 漏 2011 American Chemical Society.
语种	英语
出版者	American Chemical Society
内容类型	期刊论文
源URL	[http://dspace.xmu.edu.cn/handle/2288/89516]
专题	化学化工－已发表论文
推荐引用方式 GB/T 7714	Liao, Xinl,Long, Dong,Li, Da-Wei,et al. Probing side-chain dynamics in proteins by the measurement of nine deuterium relaxation rates per methyl group[J]. http://dx.doi.org/10.1021/jp209304c,2012.
APA	Liao, Xinl,Long, Dong,Li, Da-Wei,Br眉schweiler, Rafael,Tugarinov, Vitali,&廖新丽.(2012).Probing side-chain dynamics in proteins by the measurement of nine deuterium relaxation rates per methyl group.http://dx.doi.org/10.1021/jp209304c.
MLA	Liao, Xinl,et al."Probing side-chain dynamics in proteins by the measurement of nine deuterium relaxation rates per methyl group".http://dx.doi.org/10.1021/jp209304c (2012).