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Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy

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Book cover Protein Complex Assembly

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1764))

Abstract

In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the binding affinity from a quantitative analysis of the experimental data. In particular, we discuss the appearance of NMR spectra in different chemical exchange regimes (fast, intermediate, and slow) and how these regimes affect NMR data analysis.

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Author information

Authors and Affiliations

  1. School of Biosciences, University of Kent, Canterbury, UK

    Jose Luis Ortega-Roldan

  2. Univ. Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France

    Martin Blackledge & Malene Ringkjøbing Jensen

Authors
  1. Jose Luis Ortega-Roldan
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  2. Martin Blackledge
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  3. Malene Ringkjøbing Jensen
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Corresponding author

Correspondence to Malene Ringkjøbing Jensen .

Editor information

Editors and Affiliations

  1. MRC Human Genetics Unit, Institute of Genetics & Molecular Medicine, University of Edinburgh, Edinburgh, United Kingdom

    Joseph A. Marsh

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Ortega-Roldan, J.L., Blackledge, M., Jensen, M.R. (2018). Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy. In: Marsh, J. (eds) Protein Complex Assembly. Methods in Molecular Biology, vol 1764. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7759-8_5

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  • DOI: https://doi.org/10.1007/978-1-4939-7759-8_5

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7758-1

  • Online ISBN: 978-1-4939-7759-8

  • eBook Packages: Springer Protocols

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