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Protein Conformational Flexibility from Structure‐Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin |
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| Authors: | Loïc Salmon Guillaume Bouvignies Dr. Phineus Markwick Dr. Nils Lakomek Dr. Scott Showalter Dr. Da‐Wei Li Dr. Korvin Walter Christian Griesinger Prof. Rafael Brüschweiler Prof. Martin Blackledge Dr. |
| Affiliation: | 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)?438‐789‐554;2. Department of NMR‐Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Goettingen (Germany);3. Chemical Sciences Laboratory, Department of Chemistry and Biochemistry and National High Magnetic Field Laboratory (NHMFL), Florida State University, Tallahassee, FL 32306 (USA) |
| Abstract: | A robust procedure for the determination of protein‐backbone motions on time scales of pico‐ to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N? HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular‐dynamics trajectory of ubiquitin (red).  |
| Keywords: | Gaussian axial fluctuation molecular dynamics NMR spectroscopy protein dynamics residual dipolar coupling |