Conformational Propensities of Intrinsically Disordered Proteins from NMR Chemical Shifts

Authors

  • Jaka Kragelj,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale CEA-CNRS-UJF UMR 5075, 41, rue Jules Horowitz, 38027 Grenoble (France)
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  • Dr. Valéry Ozenne,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale CEA-CNRS-UJF UMR 5075, 41, rue Jules Horowitz, 38027 Grenoble (France)
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  • Dr. Martin Blackledge,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale CEA-CNRS-UJF UMR 5075, 41, rue Jules Horowitz, 38027 Grenoble (France)
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  • Dr. Malene Ringkjøbing Jensen

    Corresponding author
    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale CEA-CNRS-UJF UMR 5075, 41, rue Jules Horowitz, 38027 Grenoble (France)
    • Protein Dynamics and Flexibility, Institut de Biologie Structurale CEA-CNRS-UJF UMR 5075, 41, rue Jules Horowitz, 38027 Grenoble (France)

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Abstract

The realization that a protein can be fully functional even in the absence of a stable three-dimensional structure has motivated a large number of studies describing the conformational behaviour of these proteins at atomic resolution. Here, we review recent advances in the determination of local structural propensities of intrinsically disordered proteins (IDPs) from experimental NMR chemical shifts. A mapping of the local structure in IDPs is of paramount importance in order to understand the molecular details of complex formation, in particular, for IDPs that fold upon binding or undergo structural transitions to pathological forms of the same protein. We discuss experimental strategies for the spectral assignment of IDPs, chemical shift prediction algorithms and the generation of representative structural ensembles of IDPs on the basis of chemical shifts. Additionally, we highlight the inherent degeneracies associated with the determination of IDP sub-state populations from NMR chemical shifts alone.

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