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
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.