Kurt Wuthrich

Kurt Wüthrich studied molecular structural biology and structural genomics, and developed the nuclear magnetic resonance (NMR) method for determining the three-dimensional structure of proteins and nucleic acids in an artificial solution that closely resembles the conditions found in living cells.

In 2002, he was awarded the Nobel Prize in Chemistry “his development of nuclear magnetic resonance spectroscopy for determining the three-dimensional structure of biological macromolecules in solution”.

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Kurt Wuthrich
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1983 Shield of the Faculty of Medicine, Tokyo University, Japan

1990 Stein and Moore Award of the Protein Society, USA

1991 Louisa Gross Horwitz Prize, Columbia University, New York, USA

1991 Gilbert Newton Lewis Medal, University of California, Berkeley, USA

1992 Marcel Benoist-Preis Award, by Swiss Confederation

1993 Distinguished Service Award, The Miami Bio/Technology Winter Symposia, USA

1993 Prix Louis Jeantet de Médecine, Fondation Louis Jeantet, Geneva, Switzerland

1996 Kaj Linderstrøm-Lang Prize, Carlsberg Foundation, Copenhagen, Denmark

1997 Eminent Scientist award of RIKEN, Tokyo, Japan

1998 Kyoto Prize in Advanced Technology, Inamori Foundation, Kyoto, Japan

1999 Günther Laukien Prize, Experimental NMR Conference (ENC), USA

2002 Nobel Prize in Chemistry

2002 World ‘Future’ Award, The World Awards, Wien, Austria

2002 Swiss ‘Society’ Award, The Swiss Awards, Zürich, Switzerland

2008 Johannes M. Bijvoet Medal, Utrecht University, Utrecht, The Netherlands

2009 Jabir ibn Hyyan (Geber) Medal, Saudi Chemical Society

2010 Ralph and Helen Oesper Award, University of Cincinnati, Cincinnati, OH, USA

1. Wüthrich, K. (2001) Nat. Struct. Biol. 8, 923–925. The way to NMR structures of proteins.
2. Pellecchia, M., Sem, D. S., Wüthrich, K. (2002) Nat. Rev. Drug Discovery 1, 211–219. NMR in drug discovery.
3. Luginbühl, P. and Wüthrich, K (2002) Progr. Nucl. Magn. Reson. Spect.40, 199–247. Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules.
4. Herrmann T., Güntert P. and Wüthrich, K. (2002) J. Biomol. NMR 24, 171–189. Protein NMR structure determination with automated NOE-identification in the NOESY Spectra using the new software ATNOS.
5. Etezady-Esfarjani, T., Peti, W. and Wüthrich, K. (2003) J. Biomol. NMR25, 167–168. Letter to the Editor: NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima.
6. Etezady-Esfarjani, T., Herrmann, T., Peti, W., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J. Biomol. NMR 29, 403 – 406. NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis.
7. Almeida, M.S., Peti, W. and Wüthrich, K. (2004) J. Biomol. NMR 29, 453–454. Letter to the Editor: 1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima.
8. Peti, W., Etezady-Esfarjani, T., Herrmann, T., Klock, H.E., Lesley, S.A. and Wüthrich, K. (2004) J . Struct. Funct. Genomics 5, 205–215. NMR for structural proteomics of Thermotoga maritima: screening and structure determination.
9. Almeida, M.S., Peti, W. and Wüthrich, K. (2004) J. Biomol. NMR 29, 453– 454. Letter to the Editor: 1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima.
10. Peti, W., Norcross, J., Eldridge, G. and O’Neil-Johnson, M. (2004) J. Am. Chem. Soc. 126, 5873 – 5878. Biomolecular NMR using a microcoil NMR probe – new technique for the chemical shift assignment of aromatic side chains in proteins.
11. Kelker, M.S., Foss, T.R., Peti, W., Teyton, L., Kelly, J.W., Wüthrich, K. and Wilson, I.A. (2004) J. Mol. Biol. 342, 1237– 1248. Crystal structure of human triggering receptor expressed on myeloid cells 1 (TREM-1) at 1.47 Ǻ.
12. Page, R., Peti, W., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 1901 – 1905. NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.
13. Peti, W., Herrmann, T., Zagnitko, O., Grzechnik, S.K. and Wüthrich, K. (2005) Proteins: Struct. Funct. Bioinform. 59, 387–390. NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
14. Columbus, L., Peti, W., Etezady-Esfarjani, T., Herrmann, T. and Wüthrich, K. (2005) Proteins: Struct. Funct. Bioinform. 60, 552–557. NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
15. Horst, R., Bertelsen, E.B., Fiaux, J., Wider, G., Horwich, A.L. and Wüthrich, K. (2005) Proc. Natl. Acad. Sci. USA 102, 12748–12753. Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
16. Peti, W., Johnson, M.A., Herrmann, T., Neuman, B.W., Buchmeier, M.J., Nelson, M., Joseph, J., Page, R., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2005) J. Virol. 79, 12905– 12913. Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.
17. Almeida, M.S., Herrman, T., Peti, W., Wilson, I.A. and Wüthrich, K. (2005) Protein Sci. 14, 2880–2886. NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: Implications for 216 homologous DUF59 proteins.
18. Baker, K.A., Hilty, C., Peti, W., Prince, A., Pfaffinger, P.J., Wider, G., Wüthrich, K. and Choe, S. (2006) Biochemistry 45, 1663–1672. NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain.
19. Peti, W., Page, R., Moy, K., O’Neil-Johnson, M., Wilson, I.A., Stevens, R.C. and Wüthrich, K. (2005) J. Struct. Funct. Genom. 6, 259–267.Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR.
20. Etezady-Esfarjani, T., Herrmann, T., Horst, R. and Wüthrich, K. (2006) J. Biomol. NMR 34, 3 – 11. Automated protein NMR structure determination in crude cell-extract.
21. Columbus, L., Lipfert, J., Klock, H., Millett, I., Doniach, S. and Lesley, S.A. (2006) Protein Sci. 15, 961 – 975. Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination.
22. Johnson, M., Peti, W., Herrmann, T., Wilson, I. and Wüthrich, K. (2006) Protein Sci. 15, 1030 –1041. Solution structure of As11650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.
23. Almeida, M. S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9018-9. NMR assignment of the SARS-CoV protein nsp1.
24. Serrano, P., Almedia, M.S., Johnson, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9017-x. NMR assignment of the protein nsp3a from SARS-CoV.
25. Etezady-Esfarjani, T., Placzek, W.J., Herrmann, T. and Wüthrich, K. (2006) Magn. Reson. Chem. 44, S61–S70. Solution structures of the putative anti-σ-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.
26. Horst, R., Wider, G., Fiaux, J., Bertelsen, E.B., Horwich, A.L. and Wüthrich, K. (2006) Proc. Natl. Acad. Sci. USA 103, 15445–15450. Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.
27. Placzek, W.J., Almeida, M.A. and Wüthrich, K. (2006) J. Biomol. NMR, DOI 10.1007/s10858-006-9042-9. NMR assignment of a human cancer-related nucleoside triphosphatase.
28. Johnson, M.A., Southworth, M.W., Herrmann, T., Brace, L., Perler, F.B. and Wüthrich, K. (2007) Protein Sci. 16, 1316–1328. NMR structure of a Klba intein precursor from Methanococcus jannaschii.
29. Serrano, P., Johnson, M.A., Almeida, M.S., Horst, R., Herrmann, T., Joseph, J.S., Neuman, B.W., Subramanian V., Saikatendu, K.S., Buchmeier, M.J., Stevens, R.C., Kuhn, P. and Wüthrich, K. (2007)J.Virol. 81, 12049–12060.Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
30.Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B. and Wüthrich, K. (2007) Biomol. NMR Assign. 1, 191–194. NMR assignment of the domain 513–651 from the SARS-CoV nonstructural protein nsp3.
31. Horst, R., Fenton, W.A., Englander, W.S., Wüthrich, K. and Horwich A.L. (2007) Proc. Natl. Acad. Sci. USA 104 , 20788–20792. Folding trajectories of human dihydrofolate reductase inside the GroEL-GroES chaperonin cavity and free in solution.
32. Pedrini, B., Placzek, W.J., Koculi, E., Alimenti, C., LaTerza, A., Luporini, P. and Wüthrich, K. (2007) J. Mol. Biol.372, 277–286. Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from the antarctic ciliate Euplotes nobilii.
33. Zhang, Q., Horst, R., Geralt, M., Ma, X., Hong, W., Finn, M.G. Stevens, R. and Wüthrich, K. (2008) J. Am. Chem. Soc. 130, 7357–7363. Microscale NMR screening of new detergents for membrane protein structural biology.
34. Neuman, B.W., Joseph, J.S., Saikatendu, K.S., Serrano, P., Chatterjee, A., Johnson, M.A., Liao, L., Klaus, J.P., Yates, J.R., Wüthrich, K., Stevens, R., Buchmeier, M.J. and Kuhn, P. (2008) J.Virol. 82, 5279–5294. Proteomics analysis unravels the functional repertoire of Coronavirus nonstructural proten 3.
35. Serrano, P., Johnson, M.A., Chatterjee, A., Pedrini, B. and Wüthrich, K. (2008) Biomol. NMR Assign. 2, 135–138. NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV.
36. Chatterjee, A., Johnson, M.A., Serrano, P., Pedrini, B., Joseph, J.J., Neuman, B.W., Saikatendu, K., Buchmeier, M.J., Kuhn, P. and Wüthrich, K. (2009) J. Virol. 83, 1823–1836. NMR structure shows that the SARS-unique domain contains a macrodomain fold.



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  • Postings

    Visiting Professor of Structural Biology
    The Scripps Research Institute

    Professor of Biophysics
    ETH Zurich