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Correlated motions of successive amide N-H bonds in proteins

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Abstract

New nuclear magnetic resonance (NMR) methods are described for the measurement of cross-correlation rates of zero- and double-quantum coherences involving two nitrogen nuclei belonging to successive amino acids in proteins and peptides. Rates due to the concerted fluctuations of two NHN dipole-dipole interactions and to the correlated modulations of two nitrogen chemical shift anisotropies have been obtained in a sample of doubly labeled Ubiquitin. Ambiguities in the determination of dihedral angles can be lifted by comparison of different rates. By defining a heuristic order parameter, experimental rates can be compared with those expected for a rigid molecule. The cross-correlation order parameter that can be derived from a model-free approach can be separated into structural and dynamic contributions.

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Authors and Affiliations

  1. Département de chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231, Paris cedex 05, France

    Philippe Pelupessy & Geoffrey Bodenhausen

  2. 1015, Lausanne, Switzerland

    Sapna Ravindranathan & Geoffrey Bodenhausen

Authors
  1. Philippe Pelupessy
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  2. Sapna Ravindranathan
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  3. Geoffrey Bodenhausen
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Pelupessy, P., Ravindranathan, S. & Bodenhausen, G. Correlated motions of successive amide N-H bonds in proteins. J Biomol NMR 25, 265–280 (2003). https://doi.org/10.1023/A:1023076212536

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