Characterization of dynamic processes in proteins by combining solid- and solutionstate NMR spectroscopy
Zusammenfassung der Projektergebnisse
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. In this proposal, we combined solution- and MAS solid-state NMR data to probe these dynamic processes. We compared the relaxation properties of nuclear spins in the solid-state and in solution. While substantial evidences exist that the dynamic behaviour 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. We found that dynamics is fundamentally similar in solution and in the solid-state. Our approach shows how the existing ‘time-scale gap’ and extend the boundaries of dynamics studies by NMR can be bridged.
Projektbezogene Publikationen (Auswahl)
- High resolution proton detected protoncarbon correlation spectra of a protein in MAS solid-state NMR spectroscopy, J. Am. Chem. Soc. 128, 12620-12621 (2006)
Agarwal, V., Diehl, A., Skrynnikov, N., Reif, B.
- Protein Side-Chain Dynamics Observed by Solution- and Solid-state NMR: Comparative Analysis of Methyl 2H Relaxation Data, J. Am. Chem. Soc. 128, 12354- 12355 (2006)
Reif, B., Xue, Y., Agarwal, V., Pavlova, M. S., Hologne, M., Diehl, A., Ryabov, Y. E., Skrynnikov, N. R.
- Combined Analysis of 15N Relaxation Data from Solid- and Solution-State NMR Spectroscopy, J. Am. Chem. Soc. 129, 12594-12595 (2007)
Chevelkov, V., Zhuravleva, A. V., Xue, Y., Reif, B., Skrynnikov, N. R.
- Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure, J. Am. Chem. Soc. 129, 6827-6838 (2007)
Xue, Y., Pavlova, M. S., Ryabov, Y. E., Reif, B., Skrynnikov, N. R.
- Protein side-chain dynamics as observed by solution- and solid-state NMR: a similarity revealed. J. Am. Chem. Soc. 130, 16611-16621 (2008)
Agarwal, V., Xue, Y., Reif, B., Skrynnikov N.R.
- Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics, J. Am. Chem. Soc. 132, 5015-5017 (2010)
Chevelkov, V., Xue, Y., Linser, R., Skrynnikov, N.R., Reif, B.
