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

机译：残余偶极耦合作为研究泛素分子识别的工具

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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.

机译：NMR光谱中的RDC（残留偶极偶合）提供了与NMR弛豫方法互补的有关蛋白质动力学的信息，尤其是在蛋白质相关时间τc和50μs之间以前无法访问的时间窗口中。对于泛素，可以使用基于RDC的技术检测蛋白质骨架的新运动方式。发现基于这些RDC值的泛素集合体包含泛素在结合不同的识别蛋白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来自46个X射线结构。因此，对于其他蛋白的遍在蛋白识别，构象选择而不是诱导拟合似乎是主要机制。

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Lakomek, N.; Lange, O.; Walter, K.; Farès, C.; Eggers, D.; Lunkenheimer, P.; Meiler, J.; Grubmüller, H.; Becker, S.; de Groot, B.; Griesinger, C.;
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年度 2008
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1. Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex [J] . Ana I. Azuaga, Bernhard Brutscher, Jose Luis Ortega-Roldan, Nucleic acids research . 2009,第9期

机译：通过滴定NMR残留偶极偶合的精确表征弱大分子相互作用：在CD2AP SH3-C：泛素复合物中的应用
2. Quantitative Conformational Analysis of Partially Folded Proteins from Residual Dipolar Couplings: Application to the Molecular Recognition Element of Sendai Virus Nucleoprotein [J] . Malene Ringkjobing Jensen, Klaartje Houben, Ewen Lescop, Journal of the American Chemical Society . 2008,第25期

机译：残留偶极联结部分折叠的蛋白质的定量构象分析：在仙台病毒核蛋白的分子识别元件中的应用。
3. Structure and molecular ordering extracted from residual dipolar couplings: A molecular dynamics simulation study [J] . Baltzar Stevensson, Andrei V.Komolkin, Dick Sandstrom, The Journal of Chemical Physics . 2001,第5期

机译：从残余偶极偶合中提取的结构和分子有序：分子动力学模拟研究
4. MEASUREMENT AND APPLICATION OF RESIDUAL DIPOLAR COUPLINGS IN MOLECULAR MECHANICS SIMULATIONS ON EFRAPEPTIN C [C] . Thomas Huber, Burkhard Luy, Christoph Freudenberger the European Peptide Symposium . 2007

机译：EFRapeptin C的分子力学模拟中残留双极联轴器的测量与应用
5. A Residual Dipolar Coupling analysis of methyl containing side chains in ubiquitin. [D] . Sheppard, Devon. 2009

机译：遍在蛋白中含甲基侧链的残留偶极耦合分析。
6. Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex [O] . Jose Luis Ortega-Roldan, Malene Ringkjøbing Jensen, Bernhard Brutscher, 2009

机译：通过滴定NMR残留偶极偶合的精确表征弱大分子相互作用：应用于CD2AP SH3-C：泛素复合物
7. Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex [O] . Ortega-Roldan, Jose Luis, Jensen, Malene Ringkjøbing, Brutscher, Bernhard, 2009

机译：通过滴定NMR残留偶极偶合的精确表征弱大分子相互作用：应用于CD2AP SH3-C：泛素复合物

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

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