Hands-on tour of protein NMR spectroscopy
Structural and temporal information of proteins is critical to understanding their function. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique because it is capable of providing such information, while maintaining atomic resolution. In addition, solution NMR provides an avenue to study biological macromolecules in more non-invasive and physiologically relevant conditions as compared to other spectroscopic techniques.
Although in the past the use of NMR spectroscopy was limited to relatively small proteins, technical advances during the past decades have opened the doors to the study of larger systems such as membrane proteins. Besides the determination of the 3D structure of proteins, NMR is widely used to characterize dynamic properties over a broad range of timescales spanning from picoseconds to hours. Methods have been developed that even allow the characterization of lowly populated states that can have direct functional roles.
In addition to an introductory lecture, this course provides a hands-on opportunity for participants under the supervision of two PhD students participating also at the Horizons meeting. Technical aspects of how to conduct and set up solution NMR experiments will be discussed. Further, the participants will carry out experiments demonstrating the sensitivity of NMR towards molecular interactions using ubiquitin as a model system, and an example of modern methods to study large molecular weight systems will be given.
(1) Lange, O., Lakomek, N. A., Farès, C., Schröder, G.,Becker, S., Meiler, J., Grubmüller, H., Griesinger, C., de Groot, B.: Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science, 2008, 320, 1471-1475
(2) Ban, D., M.F. Funk, R. Gulich, D. Egger, T. M. Sabo, K.F.A. Walter, R. B. Fenwick, K. Giller, F, Pichierri, B.L. de Groot, O. F. Lange, H. Grubmüller, X. Salvatella, M. Wolf, A. Loidl, R. Kree, S. Becker, N.-A. Lakomek, D. Lee, P. Lunkenheimer, C. Griesinger: Kinetics of Conformational Sampling in Ubiquitin. Angew. Chem. Int. Ed. 50, 11437-11440 (2011)
(3) Bayrhuber, M., Meins, T., Habeck, M., Becker, S.,Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., Zeth, K. Structure of the human voltage-dependent anion channel, Proc. Natl. Acad. Sci. USA 105, 15370-5 (2008)
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