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Residual dipolar couplings as a tool to study molecular recognition of ubiquitin

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Lakomek,  N. A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

Walter,  K.F.A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Farès,  C.
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;
University Health Network, Max Bell Research Center, Toronto, Canada, ;

Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Lakomek, N. A., Lange, O., Walter, K., Farès, C., Eggers, D., Lunkenheimer, P., et al. (2008). Residual dipolar couplings as a tool to study molecular recognition of ubiquitin. Biochemical Society Transactions (London), 36(6), 1433-1437. doi:10.1042/BST0361433.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-4A12-F
Abstract
RDCs (residual dipolar couplings) in NMR spectroscopy provide information about protein dynamics complementary to NMR relaxation methods, especially in the previously inaccessible time window between the protein correlation time τc and 50 μs. For ubiquitin, new modes of motion of the protein backbone could be detected using RDC-based techniques. An ensemble of ubiquitin based on these RDC values is found to comprise all different conformations that ubiquitin adopts upon binding to different recognition proteins. These conformations in protein–protein complexes had been derived from 46 X-ray structures. Thus, for ubiquitin recognition by other proteins, conformational selection rather than induced fit seems to be the dominant mechanism.