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

Vugmeyster, L. ; Bodenhausen, G.

In: Applied Magnetic Resonance, 2005, vol. 28, no. 1-2, p. 147-163

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    Titre
    • Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates
    Auteur
    • Vugmeyster, L.. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland
    • Bodenhausen, G.. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Applied Magnetic Resonance, 2005, vol. 28, no. 1-2, p. 147-163. Springer-Verlag
    Autre version électronique
    Classification
    • Physique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:321431
    Summary
    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