Reto Horst , PhD.

rhorst@scripps.edu

phone: +1 858 784 2726
fax     : +1 858 784 8014 

Research Interests

My main interests focus on structure determinations of biomolecules in solution by NMR spectroscopy in the context of structural proteomics, studies on chaperone-mediated folding pathways of globular proteins and technical aspects of NMR spectroscopy.

Curriculum Vitae

2003 Ph. D. (Physics), ETH Zurich, Switzerland.

2003 – 2004 Postdoctoral Training, ETH Zurich, Switzerland.

2004 – 2005 Research Associate, The Scripps Research Institute, La Jolla, CA, USA

2005 – 2006 Senior Research Associate, The Scripps Research Institute, La Jolla, CA, USA

2006 – present Staff Scientist, The Scripps Research Institute, La Jolla, CA, USA

Publications

1. 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.

2. 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.

3. 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.

4. Hiller, S., Wider, G., Etezady-Esfarjani, T., Horst, R. and W üthrich, K. (2005) J. Biomol. NMR. 32: 61–70. Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures.

5. Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorf, P., Jelesarov, I., Grütter, M.G., Wüthrich, K., Glockshuber, R. and Capitani, G. (2005) EMBO J. 24, 2075–2086. Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD.

6. Lee, D., Damberger, F., Guihong, P., Horst, R., Güntert, P., Nikonova, L., Leal, W. and Wüthrich, K. (2002) FEBS Lett. 531, 314–318. NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.

7. Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. and Wüthrich, K. (2001) Proc. Natl. Acad. Sci. USA 98, 14374–14379. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release.

8. Horst, R., Damberger, F., Peng, G., Nikonova, L., Leal, W.S. and Wüthrich, K. (2001) J. Biomol. NMR 19, 79 – 80. NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.

9. Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S. and Wüthrich, K. (2000) Protein Sci. 9, 1038–1041. NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori.