Inside Back Cover: Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins (Angew. Chem. Int. Ed. 2/2013)

Authors

  • Dr. Jie-rong Huang,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    Search for more papers by this author
  • Valéry Ozenne,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    Search for more papers by this author
  • Dr. Malene Ringkjøbing Jensen,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    Search for more papers by this author
  • Dr. Martin Blackledge

    Corresponding author
    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    • Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    Search for more papers by this author

Abstract

original image

NMR spectroscopy is a powerful method for studying disordered proteins, providing atomic resolution and ensemble-averaged information. In their Communication on page 687 ff., M. Blackledge et al. show that by analyzing local and long-range effects, residual dipolar couplings can be determined up to six orders of magnitude faster than by existing techniques.

Cartoon 1.

Ancillary