Lakomek Nils-Alexander, Lange Oliver F, Walter Korvin F A, Farès Christophe, Egger Dalia, Lunkenheimer Peter, Meiler Jens, Grubmüller Helmut, Becker Stefan, de Groot Bert L, Griesinger Christian
Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Biochem Soc Trans. 2008 Dec;36(Pt 6):1433-7. doi: 10.1042/BST0361433.
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.
核磁共振光谱中的剩余偶极耦合（RDCs）提供了有关蛋白质动力学的信息，是对核磁共振弛豫方法的补充，特别是在蛋白质相关时间τc和50微秒之间以前无法达到的时间窗口内。对于泛素，可以使用基于RDC的技术检测蛋白质主链的新运动模式。基于这些RDC值的泛素集合被发现包含泛素与不同识别蛋白结合时所采用的所有不同构象。蛋白质-蛋白质复合物中的这些构象源自46个X射线结构。因此，对于其他蛋白质对泛素的识别，构象选择而非诱导契合似乎是主要机制。
