recent publications

• academic article

  • Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K. Nmr assignment and secondary structure determination of an octameric 110 kda protein using trosy in triple resonance experiments Journal of the American Chemical Society  2000 122:7543-7548  DOI:10.1021/ja0003268
  • Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K. C-13 -constant-time n-15,h-1 -trosy-hnca for sequential assignments of large proteins Journal of Biomolecular NMR  1999 14:85-88  DOI:10.1023/a:1008346931993  PMID:10382310
  • Salzmann, M., Wider, G., Pervushin, K., Senn, H., Wuthrich, K. Trosy-type triple-resonance experiments for sequential NMR assignments of large proteins Journal of the American Chemical Society  1999 121:844-848  DOI:10.1021/ja9834226
  • Salzmann, M., Pervushin, K., Wider, G., Senn, H., Wuthrich, K. Trosy in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins Proceedings of the National Academy of Sciences of the United States of America  1998 95:13585-13590  DOI:10.1073/pnas.95.23.13585  PMID:9811843
  • Altmann, S., Labhardt, A. M., Senn, H., Wuthrich, K. Sequence-specific h-1, c-13 and n-15 assignment of the tmp-resistant dihydrofolate reductase mutant dhfr(f98y) in the ternary complex with tmp and nadph Journal of Biomolecular NMR  1997 9:445-446  DOI:10.1023/a:1018315131994  PMID:9255948
  • Senn, H., Loosli, H. R., Sanner, M., Braun, W. Conformational studies of cyclic peptide structures in solution from h-1-NMR data by distance geometry calculation and restrained energy minimization Biopolymers  1990 29:1387-1400  DOI:10.1002/bip.360291006  PMID:2361151
  • Sanner, M., Widmer, A., Senn, H., Braun, W. Geom - a new tool for molecular modeling based on distance geometry calculations with NMR data Journal of Computer-Aided Molecular Design  1989 3:195-210  DOI:10.1007/bf01533068  PMID:2585001
  • Senn, H., Werner, B., Messerle, B. A., Weber, C., Traber, R., Wuthrich, K. Stereospecific assignment of the methyl (1)H-NMR lines of valine and leucine in polypeptides by nonrandom (13)C labeling FEBS Letters  1989 249:113-118  DOI:10.1016/0014-5793(89)80027-4
  • Neri, D., Szyperski, T., Otting, G., Senn, H., Wuthrich, K. Stereospecific nuclear magnetic-resonance assignments of the methyl-groups of valine and leucine in the DNA-binding domain of the 434-repressor by biosynthetically directed fractional c-13 labeling Biochemistry  1989 28:7510-7516  DOI:10.1021/bi00445a003  PMID:2692701
  • Senn, H., Eugster, A., Otting, G., Suter, F., Wuthrich, K. N-15-labeled p22 c2 repressor for nuclear-magnetic-resonance studies of protein-DNA interactions European Biophysics Journal with Biophysics Letters  1987 14:301-306  PMID:3552643
  • Senn, H., Otting, G., Wuthrich, K. Protein-structure and interactions by combined use of sequential NMR assignments and isotope labeling Journal of the American Chemical Society  1987 109:1090-1092  DOI:10.1021/ja00238a016
  • Otting, G., Senn, H., Wagner, G., Wuthrich, K. Editing of 2d h-1-NMR spectra using x half-filters - combined use with residue-selective n-15 labeling of proteins Journal of Magnetic Resonance  1986 70:500-505  DOI:10.1016/0022-2364(86)90144-7
  • Senn, H., Wuthrich, K. Amino-acid-sequence, hem-iron coordination geometry and functional-properties of mitochondrial and bacterial c-type cytochromes Quarterly Reviews of Biophysics  1985 18:111-134  PMID:3006116
  • Senn, H., Cusanovich, M. A., Wuthrich, K. (1)H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555 Biochimica et Biophysica Acta  1984 785:46-53  DOI:10.1016/0167-4838(84)90232-2
  • Senn, H., Bohme, H., Wuthrich, K. Studies of the solution conformation of Spirulina platensis cytochrome c-553 by (1)H-nuclear magnetic resonance and circular dichroism Biochimica et Biophysica Acta  1984 789:311-323  DOI:10.1016/0167-4838(84)90187-0
  • Senn, H., Billeter, M., Wuthrich, K. The spatial structure of the axially bound methionine in solution conformations of horse ferrocytochrome-c and pseudomonas-aeruginosa ferrocytochrome-c-551 by h-1-NMR European Biophysics Journal with Biophysics Letters  1984 11:3-15  PMID:6088217
  • Senn, H., Wuthrich, K. A new spatial structure for the axial methionine observed in cytochrome c5 from pseudomonas-mendocina - correlations with the electronic-structure of heme-c Biochimica et Biophysica Acta  1983 747:16-25  DOI:10.1016/0167-4838(83)90115-2  PMID:6309240
  • Senn, H., Wuthrich, K. Conformation of the axially bound ligands of the heme iron and electronics structure of heme c in the cytochromes c-551 from Pseudomonas mendocina and Pseudomonas stutzeri and in cytochrome c2 from Rhodospirillum rubrum Biochimica et Biophysica Acta  1983 746:48-60  DOI:10.1016/0167-4838(83)90009-2
  • Senn, H., Guerlesquin, F., Bruschi, M., Wuthrich, K. Coordination of the heme iron in the low-potential cytochromes c-553 from desulfovibrio-vulgaris and desulfovibrio-desulfuricans - different chirality of the axially bound methionine in the oxidized and reduced states Biochimica et Biophysica Acta  1983 748:194-204  DOI:10.1016/0167-4838(83)90295-9  PMID:6313059
  • Senn, H., Eugster, A., Wuthrich, K. Determination of the coordination geometry at the heme iron in 3 cytochromes-c from saccharomyces-cerevisiae and from candida-krusei based on individual h-1-NMR assignments for heme-c and the axially coordinated amino-acids Biochimica et Biophysica Acta  1983 743:58-68  DOI:10.1016/0167-4838(83)90418-1  PMID:6297596
  • Senn, H., Wuthrich, K. Individual h-1-NMR assignments for the heme groups and the axially bound amino-acids and determination of the coordination geometry at the heme iron in a mixture of 2 isocytochromes-c-551 from rhodopseudomonas-gelatinosa Biochimica et Biophysica Acta  1983 743:69-81  DOI:10.1016/0167-4838(83)90419-3  PMID:6297597
  • Senn, H., Keller, R. M., Wuthrich, K. Different chirality of the axial methionine in homologous cytochromes-c determined by h-1-NMR and cd spectroscopy Biochemical and Biophysical Research Communications  1980 92:1362-1369  DOI:10.1016/0006-291x(80)90436-2  PMID:6245651