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1H,13C-1H,1H Dipolar Cross-correlated Spin Relaxation in Methyl Groups

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Abstract

Relaxation in methyl groups is strongly influenced by cross-correlated interactions involving the methyl dipoles. One of the major interference effects results from intra-methyl 1H-13C, 1H-1H dipolar interactions, leading to significant differences in the relaxation of certain multiplet components that contribute to double- and zero-quantum 1H-13C spectra. NMR experiments are presented for the measurement of this differential relaxation effect. It is shown that this difference in relaxation between double- and zero-quantum multiplet components can be used as a sensitive reporter of side chain dynamics and that accurate methyl axis order parameters can be measured in proteins that tumble with correlation times greater than approximately 5 ns.

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Authors and Affiliations

  1. Protein Engineering Network Centres of Excellence and the Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario, Canada, M5S 1A8

    Vitali Tugarinov & Lewis E. Kay

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  1. Vitali Tugarinov
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  2. Lewis E. Kay
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Tugarinov, V., Kay, L.E. 1H,13C-1H,1H Dipolar Cross-correlated Spin Relaxation in Methyl Groups. J Biomol NMR 29, 369–376 (2004). https://doi.org/10.1023/B:JNMR.0000032562.07475.7f

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  • DOI: https://doi.org/10.1023/B:JNMR.0000032562.07475.7f

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