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

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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.