Volume 52, Issue 2 p. 771
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Inside Back Cover: Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins (Angew. Chem. Int. Ed. 2/2013)

Dr. Jie-rong Huang

Dr. Jie-rong Huang

Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)

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Valéry Ozenne

Valéry Ozenne

Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)

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Dr. Malene Ringkjøbing Jensen

Dr. Malene Ringkjøbing Jensen

Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)

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Dr. Martin Blackledge

Corresponding Author

Dr. Martin Blackledge

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
First published: 11 December 2012
Citations: 2

Graphical Abstract

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.

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