期刊
JOURNAL OF CHEMICAL PHYSICS
卷 133, 期 1, 页码 -出版社
AIP Publishing
DOI: 10.1063/1.3454734
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A simple general expression for the NMR cross-correlated relaxation rate under anisotropic molecular tumbling is presented for globular proteins. The derivation includes effects of fast and slow motion of the interaction tensors and correlation between them. Expressions suitable for practical analysis are tailored in dependence of standard order parameters of the individual interactions. It is shown that these order parameters must be sensitive to slow motion (slower than molecular tumbling) for detection of slow correlated motion. Such order parameters are those obtained from residual dipolar couplings but not those obtained from T1, T2, and heteronuclear Nuclear Overhauser Enhancement measurements. (C) 2010 American Institute of Physics.
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