title: Residual dipolar couplings as a tool to study molecular recognition of ubiquitin.
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 tau(c) and 50 micros. 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.
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Nils-Alexander
authors.initials: NA
authors.lastname: Lakomek
authors.forename: Oliver F
authors.initials: OF
authors.lastname: Lange
authors.forename: Korvin F A
authors.initials: KF
authors.lastname: Walter
authors.forename: Christophe
authors.initials: C
authors.lastname: Farès
authors.forename: Dalia
authors.initials: D
authors.lastname: Egger
authors.forename: Peter
authors.initials: P
authors.lastname: Lunkenheimer
authors.forename: Jens
authors.initials: J
authors.lastname: Meiler
authors.forename: Helmut
authors.initials: H
authors.lastname: Grubmüller
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Bert L
authors.initials: BL
authors.lastname: de Groot
authors.forename: Christian
authors.initials: C
authors.lastname: Griesinger
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D025801:Ubiquitin