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

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Abstract

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.

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Authors and Affiliations

  1. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland

    L. Vugmeyster & G. Bodenhausen

  2. Départment de Chimie, Associé au Centre National de la Recherche Scientifique Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris cedex 05, France

    G. Bodenhausen

Authors
  1. L. Vugmeyster
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  2. G. Bodenhausen
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Vugmeyster, L., Bodenhausen, G. Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates. Appl. Magn. Reson. 28, 147–163 (2005). https://doi.org/10.1007/BF03167001

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  • DOI: https://doi.org/10.1007/BF03167001

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