Characterization of dynamic processes in proteins by combining solid- and solutionstate NMR spectroscopy

通过结合固态和溶液态 NMR 光谱来表征蛋白质的动态过程

• 批准号: 49988221
• 负责人: Professor Dr. Bernd Reif
• 金额: --
• 依托单位: Professur für Festkörper-NMR-Spektroskopie
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2007
• 资助国家: 德国
• 起止时间: 2006-12-31 至 2010-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/49988221?language=en
• 关键词: Characterization; dynamic; processes; proteins; combining

The goal of the applied research project is an integrated analysis of dynamic processes in proteins combining solution and MAS solid-state NMR spectroscopy. The combined expertise of the two applying groups is essential for the proposed project. Protein dynamics is a key element for understanding of biological function. Nuclear magnetic resonance relaxation experiments allow the characterization of these dynamic processes. Relaxation in solution is controlled by the overall tumbling of the molecule (10-9 s). Only fast motional processes (10-12-10-9 s) can be therefore probed using solution-state relaxation experiments. Motions on the time scale 10-9-10-7 s are difficult or impossible to detect by solution-state relaxation measurements. Alternative approaches using residual dipolar couplings remain under discussion. In this proposal, we suggest to combine solution- and MAS solid-state NMR data to probe these dynamic processes. We seek to determine if internal motions are changed upon transition from solution to solids. While substantial evidences exist that the dynamic behavior is similar, the spectroscopic context, on the other hand, is very different: solid-state NMR spectroscopy is sensitive to a broad range of correlation times, while solution-state NMR experiments are selective with respect to faster forms of motion. This opens up attractive possibilities for a detailed and selfcontained characterization of internal protein dynamics. The proposed work will bridge the existing ‘time-scale gap’ and extend the boundaries of dynamics studies by NMR. In the proposed study, solid-state experiments will be conducted by the group of Bernd Reif (BR), while solution work is the responsibility of Nikolai Skrynnikov’s (NS) group. The data analysis will be carried out jointly.

应用研究项目的目标是对蛋白质中的动态过程的综合分析，结合溶液和MAS固态NMR光谱。两个应用组的组合专业知识对于拟议项目至关重要。蛋白质动力学是理解生物学功能的关键要素。核磁共振松弛实验允许表征这些动态过程。溶液中的松弛由分子的整体翻滚（10-9 s）控制。因此，只能使用溶液状态弛豫实验来探测快速运动过程（10-12-10-9 s）。时间尺度上的运动10-9-10-7 S难以或无法通过解决方案状态松弛测量来检测。使用残留偶极耦合的替代方法仍在讨论中。在此提案中，我们建议将解决方案和MAS固态NMR数据结合起来，以探测这些动态过程。我们试图确定从溶液过渡到固体时是否改变了内部动作。尽管存在充分的证据表明动态行为是相似的，但另一方面，光谱环境却大不相同：固态NMR光谱对广泛的相关时间敏感，而溶液状态NMR实验对于更快的运动形式而言是选择性的。这为内部蛋白质动力学的详细且独立的表征打开了有吸引力的可能性。拟议的工作将弥合现有的“时间尺度差距”，并扩大NMR动态研究的界限。在拟议的研究中，固态实验将由Bernd Reif（BR）的小组进行，而解决方案工作则是尼古拉Skrynnikov（NS）组的责任。数据分析将共同进行。