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The Wüthrich Laboratory

Kurt Wüthrich: Research Highlights/Selected Publications

For 50 years, Wüthrich groups at the ETH Zürich, Zürich, Switzerland, Scripps Research, La Jolla, CA, USA and the iHuman Institute of ShanghaiTech University, Shanghai, China have worked on nuclear magnetic resonance spectroscopy (NMR) with biological macromolecules. Contributions include the method for macromolecular structure determination with NMR in solution and the use of the principles of transverse relaxation-optimized spectroscopy (TROSY) for NMR experiments with large supramolecular assemblies. Applications over the years were focused on differentiation in higher organisms, immune suppression and neuropathology. As of April 1, 2019, research using NMR techniques is continued at ShanghaiTech University, with a focus on G protein-coupled receptors (GPCRs). At Scripps Research and the ETH Zürich, projects on the general theme “healthcare in the ageing human societies of the 21st century” are pursued, mainly considering the impact of sarcopenia on the human healthspan.

Kurt Wüthrich: References to “Research Highlights”

Sušac, L., Eddy, M.T., Didenko, T., Stevens, R.C. and Wüthrich, K. (2019) Proc. Natl. Acad. Sci. USA 115, 12733–12738.
A2A adenosine receptor functional states characterized by 19F-NMR.
Shimada, I., Ueda, T., Kofuku, Y., Eddy, M.T. and Wüthrich, K. (2019) Nat. Rev. Drug Disc. 18, 59–82.
GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures.
Eddy, M.T., Lee, M.-Y., Gao, Z.-G., White, K.L., Didenko, T., Horst, R., Audet, M., Stanczak, P., McClary, K.M., Han, G.W., Jacobson, K.A., Stevens, R. and Wüthrich, K. (2018) Cell 172, 68–80.
Allosteric coupling of drug binding and intracellular signaling in the A2A adenosine receptor.
Liu, J.J., Horst, R., Katritch, V., Stevens, R.C. and Wüthrich, K. (2012) Science 335, 1106–1110.
Biased signaling pathways in β2-adrenergic receptor characterized by 19F-NMR.
Wüthrich, K. (2003) Angew.Chem. Int. Ed. 42, 3340−3363.
NMR studies of structure and function of biological macromolecules (Nobel Lecture).
Fiaux, J., Bertelsen, E., Horwich, A. and Wüthrich, K. (2002) Nature 418, 207–211.
NMR analysis of a 900K GroEL–GroES complex.

Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA 94, 12366–12371.
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wüthrich, K. (1996) Nature
382, 180–182.
NMR structure of the mouse prion protein domain PrP(121–231).

Otting, G., Liepinsh, E. and Wüthrich, K. (1991) Science 254, 974–980.
Protein hydration in aqueous solution.

Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.

Wüthrich, K. (1969) Proc. Natl. Acad. Sci. USA 63, 1071–1078.
High resolution proton nuclear magnetic resonance spectroscopy of cytochrome c.