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NMR Studies of Protein–Ligand Interactions

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Protein NMR Techniques

Part of the book series: Methods in Molecular Biology ((MIMB,volume 831))

Abstract

Nuclear magnetic resonance (NMR) has evolved into a powerful tool for characterizing protein–ligand interactions in solution under near physiological conditions. It is now frequently harnessed to assess the affinity and specificity of interactions; to identify binding epitopes on proteins and ligands; and to characterize the structural rearrangements induced by binding.

The first section of this chapter provides a general overview of the NMR study of protein–ligand interactions. The section is divided according to two main categories of experiments: those based on observing protein signals and those based on observing ligand signals. The next section explains two case studies performed in the authors’ laboratory. The first of these deals with the interaction between vascular endothelial growth factor and a peptidic ligand, and includes a detailed protocol of chemical shift perturbation experiments. The second one reports on the interaction between prolyl oligopeptidase and a small molecule as monitored by ligand saturation transfer difference (STD), and illustrates how NMR can be used to confirm binding and to identify the binding epitope of a ligand.

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Author information

Authors and Affiliations

  1. Parc Científic de Barcelona, Institute for Research in Biomedicine (IRB Barcelona), Barcelona, Spain

    Michael Goldflam, Teresa Tarragó & Ernest Giralt

  2. Servicios Cientifi co Tecnicos, Universitat de Barcelona, Barcelona, Spain

    Margarida Gairí

  3. Departament de Química Orgànica, Universitat de Barcelona, Barcelona, Spain

    Ernest Giralt

Authors
  1. Michael Goldflam
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  2. Teresa Tarragó
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  3. Margarida Gairí
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  4. Ernest Giralt
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Corresponding author

Correspondence to Ernest Giralt .

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Editors and Affiliations

  1. University of Albany, State University of New York, Washington Avenue 1400, Albany, 12222, New York, USA

    Alexander Shekhtman

  2. University of Albany, State University of New York, Washington Avenue 1400, Albany, 12222, New York, USA

    David S. Burz

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Goldflam, M., Tarragó, T., Gairí, M., Giralt, E. (2012). NMR Studies of Protein–Ligand Interactions. In: Shekhtman, A., Burz, D. (eds) Protein NMR Techniques. Methods in Molecular Biology, vol 831. Humana Press. https://doi.org/10.1007/978-1-61779-480-3_14

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  • DOI: https://doi.org/10.1007/978-1-61779-480-3_14

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  • Print ISBN: 978-1-61779-479-7

  • Online ISBN: 978-1-61779-480-3

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