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Study of protein dynamics in solution by measurement of 13Cα-13CO NOE and 13CO longitudinal relaxation

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Summary

13Cα-13CO homonuclear NOE and 13CO T1 relaxation were measured for a 20 kDa protein using tripleresonance pulse sequences. The experiments were sufficiently sensitive to obtain statistically significant differences in relaxation parameters over the molecule. The 13Cα-13CO cross-relaxation rate, obtained from these data, is directly proportional to an order parameter describing local motion and it is largely independent of the local correlation time. It is therefore a relatively straightforward observable for the identification of local dynamics.

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Authors and Affiliations

  1. Biophysics Research Division, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA

    Lei Zeng, Mark W. F. Fischer & Erik R. P. Zuiderweg

  2. Department of Biological Chemistry, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA

    Erik R. P. Zuiderweg

  3. Department of Physics, The University of Michigan, 930 N. University Avenue, 48109-1055, Ann Arbor, MI, USA

    Mark W. F. Fischer

Authors
  1. Lei Zeng
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  2. Mark W. F. Fischer
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  3. Erik R. P. Zuiderweg
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Zeng, L., Fischer, M.W.F. & Zuiderweg, E.R.P. Study of protein dynamics in solution by measurement of 13Cα-13CO NOE and 13CO longitudinal relaxation. J Biomol NMR 7, 157–162 (1996). https://doi.org/10.1007/BF00203826

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  • DOI: https://doi.org/10.1007/BF00203826

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