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Measurement and Analysis of NMR Residual Dipolar Couplings for the Study of Intrinsically Disordered Proteins

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Intrinsically Disordered Protein Analysis

Part of the book series: Methods in Molecular Biology ((MIMB,volume 895))

Abstract

Intrinsically disordered proteins (IDPs) are predicted to represent a significant fraction of all functional proteins. Their inherent plasticity allows them to sample more efficiently their surroundings and thereby increase the probability of interaction with one or several different biological partners. Due to their high flexibility, IDPs cannot be represented by a single, three-dimensional structure; rather, an ensemble description can be invoked, where the protein is assumed to interconvert between different conformations. This chapter focuses on the use of NMR spectroscopy to characterize the dynamic behavior of IDPs, in particular residual dipolar couplings, that provide highly sensitive tools for the study of intrinsic structural propensity and conformational transitions accompanying protein function.

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Author information

Authors and Affiliations

  1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA; CNRS, Grenoble, France

    Loïc Salmon, Malene Ringkjøbing Jensen & Martin Blackledge

  2. Centre de Biochimie Structurale, CNRS UMR 5048 - UM 1 - INSERM UMR 1054, Montpellier, France

    Pau Bernadó

Authors
  1. Loïc Salmon
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  2. Malene Ringkjøbing Jensen
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  3. Pau Bernadó
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  4. Martin Blackledge
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Corresponding author

Correspondence to Pau Bernadó .

Editor information

Editors and Affiliations

  1. Department of Molecular Medicine, College of Medicine, University of South Florida, Bruce B. Downs Blvd 12901, Tampa, 33612, Florida, USA

    Vladimir N. Uversky

  2. Dept. Biochemistry & Molecular Biology, Center for Computational Biology &, Indiana University, West 10th Street 410, Indianapolis, 46202, Indiana, USA

    A. Keith Dunker

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Salmon, L., Jensen, M.R., Bernadó, P., Blackledge, M. (2012). Measurement and Analysis of NMR Residual Dipolar Couplings for the Study of Intrinsically Disordered Proteins. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 895. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-927-3_9

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  • DOI: https://doi.org/10.1007/978-1-61779-927-3_9

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-61779-926-6

  • Online ISBN: 978-1-61779-927-3

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