Education

Ph.D. in Biophysics, Department of Physics, ETH Zürich, Switzerland, 2003

Current position

Principal Scientist, Pfizer Global Research and Development, Groton, CT, USA

Publications

1. Horst, R., Stanczak, P. and Wüthrich, K. (2014). NMR polypeptide backbone conformation of the E. coli outer membrane protein W. Structure 22(8): 1204-1209.
   
2.  Sušac, L., Horst, R. and Wüthrich, K. (2014). Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles. Chembiochem 15(7): 995-1000.
   
3.  Didenko, T., Liu, J. J., Horst, R., Stevens, R. C. and Wüthrich, K. (2013). Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs. Curr Opin Struct Biol 23(5): 740-747.
   
4.  Horst, R., Liu, J. J., Stevens, R. C. and Wüthrich, K. (2013). beta(2)-adrenergic receptor activation by agonists studied with (1)(9)F NMR spectroscopy. Angew Chem Int Ed Engl 52(41): 10762-10765.
   
5. Horst, R., Stanczak, P., Stevens, R. C. and Wüthrich, K. (2013). beta2-Adrenergic receptor solutions for structural biology analyzed with microscale NMR diffusion measurements. Angew Chem Int Ed Engl 52(1): 331-335.
   
6. Stanczak, P., Zhang, Q., Horst, R., Serrano, P. and Wüthrich, K. (2012). Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles. J Biomol NMR 54(2): 129-133.
   
7. Liu, J. J., Horst, R., Katritch, V., Stevens, R. C. and Wüthrich, K. (2012). Biased signaling pathways in beta2-adrenergic receptor characterized by 19F-NMR. Science 335(6072): 1106-1110.
   
8. Horst, R., Stanczak, P., Serrano, P. and W üthrich, K. (2012). Translational diffusion measurements by microcoil NMR in aqueous solutions of the Fos-10 detergent-solubilized membrane protein OmpX. J Phys Chem B 116(23): 6775-6780.
   
9.  Horst, R., Horwich, A. L. and W üthrich, K. (2011). Translational diffusion of macromolecular assemblies measured using transverse-relaxation-optimized pulsed field gradient NMR. J Am Chem Soc 133(41): 16354-16357.
   
10.  Koculi, E., Horst, R., Horwich, A. L. and Wüthrich, K. (2011). Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL. Protein Sci 20(8): 1380-1386.
    
11.  Jaudzems, K., Geralt, M., Serrano, P., Mohanty, B., Horst, R., Pedrini, B., Elsliger, M. A., Wilson, I. A. and Wüthrich, K. (2010). NMR structure of the protein NP_247299.1: comparison with the crystal structure. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 10): 1367-1380.
    
12. Mohanty, B., Serrano, P., Pedrini, B., Jaudzems, K., Geralt, M., Horst, R., Herrmann, T., Elsliger, M. A., Wilson, I. A. and Wüthrich, K. (2010). Comparison of NMR and crystal structures for the proteins TM1112 and TM1367. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 10): 1381-1392.
    
13.  Serrano, P., Pedrini, B., Geralt, M., Jaudzems, K., Mohanty, B., Horst, R., Herrmann, T., Elsliger, M. A., Wilson, I. A. and Wüthrich, K. (2010). Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites. Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 10): 1393-1405.
    
14.  Stanczak, P., Horst, R., Serrano, P. and W üthrich, K. (2009). NMR characterization of membrane protein-detergent micelle solutions by use of microcoil equipment. J Am Chem Soc 131(51): 18450-18456.
    
15.  Zhang, Q., Horst, R., Geralt, M., Ma, X., Hong, W. X., Finn, M. G., Stevens, R. C. and Wuthrich, K. (2008). Microscale NMR screening of new detergents for membrane protein structural biology. J Am Chem Soc 130(23): 7357-7363.
    
16. Horst, R., Fenton, W. A., Englander, S. W., Wüthrich, K. and Horwich, A. L. (2007). Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proc Natl Acad Sci U S A 104(52): 20788-20792.
    
17. 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). Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus. J Virol 81(21): 12049-12060.
    
18. Horst, R., Wider, G., Fiaux, J., Bertelsen, E. B., Horwich, A. L. and Wüthrich, K. (2006). Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures. Proc Natl Acad Sci U S A 103(42): 15445-15450.
    
19. Etezady-Esfarjani, T., Herrmann, T., Horst, R. and Wüthrich, K. (2006). Automated protein NMR structure determination in crude cell-extract. J Biomol NMR 34(1): 3-11.
    
20.  Horst, R., Bertelsen, E. B., Fiaux, J., Wider, G., Horwich, A. L. and Wüthrich, K. (2005). Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc Natl Acad Sci U S A 102(36): 12748-12753.
    
21.  Nishiyama, M., Horst, R., Eidam, O., Herrmann, T., Ignatov, O., Vetsch, M., Bettendorff, P., Jelesarov, I., Grutter, M. G., Wüthrich, K., Glockshuber, R. and Capitani, G. (2005). Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD. EMBO J 24(12): 2075-2086.
    
22. Hiller, S., Wider, G., Etezady-Esfarjani, T., Horst, R. and Wüthrich, K. (2005). Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures. J Biomol NMR 32(1): 61-70.
    
23.  Lee, D., Damberger, F. F., Peng, G., Horst, R., Guntert, P., Nikonova, L., Leal, W. S. and Wüthrich, K. (2002). NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. FEBS Lett 531(2): 314-318.
    
24. Horst, R., Damberger, F., Luginbühl, P., Güntert, P., Peng, G., Nikonova, L., Leal, W. S. and Wüthrich, K. (2001). NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proc Natl Acad Sci U S A 98(25): 14374-14379.
    
25. Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S. and Wüthrich, K. (2001). Letter to the Editor: NMR assignment of the A form of the pheromone-binding protein of Bombyx mori. J Biomol NMR 19 (1): 79-80.
    
26.  Damberger, F., Nikonova, L., Horst, R., Peng, G., Leal, W. S. and Wüthrich, K. (2000). NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori. Protein Sci 9(5): 1038-1041.