caa a22 4500 445325127 CHVBK 20180317142717.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9567-4 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9567-4 Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins [Elektronische Daten] [Rodolfo Rasia, Ewen Lescop, Javier Palatnik, Jérôme Boisbouvier, Bernhard Brutscher] It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results. Here we present a suite of time- and sensitivity optimized NMR experiments for rapid measurement of up to six RDCs per residue. Including such an RDC data set, measured in less than 24h on a single aligned protein sample, greatly improves convergence of the Rosetta-NMR protocol, allowing for overnight fold calculation of small proteins. We demonstrate the performance of our fast fold calculation approach for ubiquitin as a test case, and for two RNA-binding domains of the plant protein HYL1. Structure calculations based on simulated RDC data highlight the importance of an accurate and precise set of several complementary RDCs as additional input restraints for high-quality de novo structure determination. Springer Science+Business Media B.V., 2011 Fast NMR nationallicence RDC nationallicence Rosetta nationallicence Protein structure calculation nationallicence Rasia Rodolfo Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut Lescop Ewen Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut Palatnik Javier Instituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina aut Boisbouvier Jérôme Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut Brutscher Bernhard Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 369-378 0925-2738 51:3<369 2011 51 10858 https://doi.org/10.1007/s10858-011-9567-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9567-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rasia Rodolfo Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut NATIONALLICENCE 700 1- Lescop Ewen Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut NATIONALLICENCE 700 1- Palatnik Javier Instituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina aut NATIONALLICENCE 700 1- Boisbouvier Jérôme Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut NATIONALLICENCE 700 1- Brutscher Bernhard Institut de Biologie Structurale, Jean-Pierre Ebel CNRS/CEA/UJF, 41 rue Jules Horowitz, 38027, Grenoble Cedex, France aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 369-378 0925-2738 51:3<369 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer