Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates

  • L. Vugmeyster
  • G. Bodenhausen


The temperature dependence of nuclear magnetic resonance relaxation rates was investigated for the backbone of15N/13C labeled human ubiquitin in the temperature range of 20–50 °C. The15N autorelaxation rates give evidence that the potential energy functions for15N−HN bonds are not quadratic, in agreement with results for other proteins. Cross-correlation rates arising from correlated fluctuations of two15N−HN dipole-dipole interactions involving successive residues were obtained by the method of Pelupessy et al. (P. Pelupessy, S. Ravindranathan, G. Bodenhausen: J. Biomol. NMR 25, 265–280, 2003). The results suggest the presence of slow internal motions at 50 °C.


Nuclear Magnetic Resonance Slow Motion Residue Number Nuclear Magnetic Resonance Structure Human Ubiquitin 
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Copyright information

© Springer 2005

Authors and Affiliations

  • L. Vugmeyster
    • 1
  • G. Bodenhausen
    • 1
    • 2
  1. 1.Institut des Sciences et Ingénierie ChimiquesEcole Polytechnique Fédérale de LausanneLausanneSwitzerland
  2. 2.Départment de ChimieAssocié au Centre National de la Recherche Scientifique Ecole Normale SupérieureParis cedex 05France

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