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Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

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

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Farès,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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

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

Lange, F., Lakomek, N. A., Farès, C., Schröder, G., Walter, K., Becker, S., et al. (2008). Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution. Science Magazine, 320(5882), 1471-1475. doi:10.1126/science.1157092.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-49CE-4
Abstract
Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.