Probing methyl dynamics from 13C autocorrelated and cross-correlated relaxation

被引：0
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作者：
Zhang, Xu [1 ,2 ]
Sui, Xiaogang [3 ]
Yang, Daiwen [1 ]
机构：
[1] Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore
[2] State Key Laboratory of Magnetic Resonance and Molecular and Atomic Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China
[3] Department of Chemistry, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore
来源：
Journal of the American Chemical Society | 2006年 / 128卷 / 15期
关键词：
An understanding of side-chain motions in protein is of great interest since side chains often play an important role in protein folding and intermolecular interactions. A novel method for measuring dipole-dipole cross-correlated relaxation in methyl groups of uniformly 13C-labeled proteins without deuteration has been developed by our group. The excellent agreement between dynamic parameters of methyl groups in ubiquitin obtained from the cross-correlated relaxation and 13C spin-lattice relaxation and those derived previously from 2H relaxation data demonstrates the reliability of the method. This method was applied to the study of side-chain dynamics of human intestinal fatty acid binding protein (IFABP) with and without its ligand. Binding of oleic acid to the protein results in decreased mobility of most of the methyl groups in the binding region; whereas no significant change in mobility was observed for methyl groups in the nonbinding region. © 2006 American Chemical Society;
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页码：5073 / 5081
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