An approach to direct determination of protein dynamics from 15N NMR relaxation at multiple fields, independent of variable 15N chemical shift anisotropy and chemical exchange contributions

David Fushman, Nico Tjandra, David Cowburn

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An approach to protein dynamics analysis from 15N relaxation data is demonstrated, based on multiple-field relaxation data. This provides a direct, residue-specific determination of both the spectral density components, the 15N chemical shift anisotropy (CSA) and the conformational exchange contribution to the 15N line width. Measurements of R1, R2, and 15N{1H} NOE are used. The approach is free from any assumption about the values of the CSA or of the conformational exchange. Using this approach, the spectral densities, the values of 15N CSA, and the conformational exchange contribution to the 15N line width are directly determined from the relaxation data for human ubiquitin, collected at 360, 500, and 600 MHz. The spectral densities are analyzed in terms of the order parameter and the correlation time of local motion, using an axially symmetric overall rotational diffusion model. The residue-specific values of 15N CSA and the spectral densities obtained using this approach are in agreement with those derived previously [Fushman, Tjandra, and Cowburn. J. Am. Chem. Soc. 1998, 120, 10947-10952] from CSA/dipolar cross-correlation analysis. Accurate determination of spectral densities and order parameters from 15N relaxation may be accomplished by analysis of multiple-field data without assumption of constant CSA or zero chemical exchange contributions.

Original languageEnglish (US)
Pages (from-to)8577-8582
Number of pages6
JournalJournal of the American Chemical Society
Issue number37
Publication statusPublished - Sep 22 1999
Externally publishedYes


ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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