Structure, Dynamics, and Kinetics of Weak Protein–Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions

Authors

  • Dr. Loïc Salmon,

    1. Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
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  • Dr. José-Luis Ortega Roldan,

    1. Departamento de Química Física e Instituto de Biotecnología, Facultad de Ciencias, Universidad de Granada, Granada (Spain)
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  • Dr. Ewen Lescop,

    1. Centre de Recherche de Gif, Institut de Chimie des Substances Naturelles, CNRS, 1 Avenue de la Terrasse, 91198 Gif sur Yvette (France)
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  • Antoine Licinio,

    1. Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
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  • Prof. Nico van Nuland,

    1. Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, Brussels (Belgium)
    2. Department of Molecular and Cellular Interactions, VIB, Pleinlaan 2, 1050 Brussels (Belgium)
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  • Dr. Malene Ringkjøbing Jensen,

    Corresponding author
    1. Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
    • Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
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  • Dr. Martin Blackledge

    Corresponding author
    1. Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
    • Protein Dynamics and Flexibility, Institute de Biologie, Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027-Grenoble Cedex (France), Fax: (+33) 4-3878-9554
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  • This work was supported by the ANR (PCV Protein Motion).

Abstract

original image

Making the invisible visible: Weak protein–protein interactions play a key role in a range of essential biological processes. However, transient or ultraweak complexes cannot be studied in detail by many biophysical techniques. A method based on the measurement of 15N relaxation rates can be used to study weak protein complexes (see picture; Dzz=diffusion tensor).

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