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Devi, V. S., Sprecher, C. B., Hunziker, P., Mittl, P. R., Bosshard, H. R. & Jelesarov, I. Disulfide formation and stability of a cysteine-rich repeat protein from Helicobacter pylori. Biochemistry 45, 1599–607 (2006).
Milev, S., Bosshard, H. R. & Jelesarov, I. Enthalpic and entropic effects of salt and polyol osmolytes on site-specific protein-DNA association: the integrase Tn916-DNA complex. Biochemistry 44, 285–93 (2005).
Bosshard, H. R., Marti, D. N. & Jelesarov, I. Protein stabilization by salt bridges: concepts, experimental approaches and clarification of some misunderstandings. J. Mol. Recognit. 17, 1–16 (2004).
Cranz, S., Berger, C., Baici, A., Jelesarov, I. & Bosshard, H. R. Monomeric and dimeric bZIP transcription factor GCN4 bind at the same rate to their target DNA site. Biochemistry 43, 718–27 (2004).
Devi, V. S., Binz, H. K., Stumpp, M. T., Plückthun, A., Bosshard, H. R. & Jelesarov, I. Folding of a designed simple ankyrin repeat protein. Protein Sci. 13, 2864–70 (2004).
Marti, D. N., Bjelic, S., Lu, M., Bosshard, H. R. & Jelesarov, I. Fast folding of the HIV-1 and SIV gp41 six-helix bundles. J. Mol. Biol. 336, 1–8 (2004).
Marti, D. N. & Bosshard, H. R. Inverse electrostatic effect: electrostatic repulsion in the unfolded state stabilizes a leucine zipper. Biochemistry 43, 12436–47 (2004).
Marti, D. N. & Bosshard, H. R. Electrostatic interactions in leucine zippers: thermodynamic analysis of the contributions of Glu and His residues and the effect of mutating salt bridges. J. Mol. Biol. 330, 621–37 (2003).
Milev, S., Gorfe, A. A., Karshikoff, A., Clubb, R. T., Bosshard, H. R. & Jelesarov, I. Energetics of sequence-specific protein-DNA association: conformational stability of the DNA binding domain of integrase Tn916 and its cognate DNA duplex. Biochemistry 42, 3492–502 (2003).
Milev, S., Gorfe, A. A., Karshikoff, A., Clubb, R. T., Bosshard, H. R. & Jelesarov, I. Energetics of sequence-specific protein-DNA association: binding of integrase Tn916 to its target DNA. Biochemistry 42, 3481–91 (2003).
Gorfe, A. A., Ferrara, P., Caflisch, A., Marti, D. N., Bosshard, H. R. & Jelesarov, I. Calculation of protein ionization equilibria with conformational sampling: pK(a) of a model leucine zipper, GCN4 and barnase. Proteins 46, 41–60 (2002).
Phelan, P., Gorfe, A. A., Jelesarov, I., Marti, D. N., Warwicker, J. & Bosshard, H. R. Salt bridges destabilize a leucine zipper designed for maximized ion pairing between helices. Biochemistry 41, 2998–3008 (2002).
Renault, J. P., Bernard, A., Juncker, D., Michel, B., Bosshard, H. R. & Delamarche, E. Fabricating microarrays of functional proteins using affinity contact printing. Angew. Chem. Int. Ed. Engl. 41, 2320–3 (2002).
Bernard, A., Fitzli, D., Sonderegger, P., Delamarche, E., Michel, B., Bosshard, H. R. & Biebuyck, H. Affinity capture of proteins from solution and their dissociation by contact printing. Nat. Biotechnol. 19, 866–9 (2001).
Bosshard, H. R. Molecular recognition by induced fit: how fit is the concept? News Physiol. Sci. 16, 171–3 (2001).
Bosshard, H. R., Dürr, E., Hitz, T. & Jelesarov, I. Energetics of coiled coil folding: the nature of the transition states. Biochemistry 40, 3544–52 (2001).
Dürr, E. & Bosshard, H. R. Folding of a three-stranded coiled coil. Protein Sci. 9, 1410–5 (2000).
Marti, D. N., Jelesarov, I. & Bosshard, H. R. Interhelical ion pairing in coiled coils: solution structure of a heterodimeric leucine zipper and determination of pKa values of Glu side chains. Biochemistry 39, 12804–18 (2000).
Perozzo, R., Jelesarov, I., Bosshard, H. R., Folkers, G. & Scapozza, L. Compulsory order of substrate binding to herpes simplex virus type 1 thymidine kinase. A calorimetric study. J. Biol. Chem. 275, 16139–45 (2000).
Berger, C., Weber-Bornhauser, S., Eggenberger, J., Hanes, J., Plückthun, A. & Bosshard, H. R. Antigen recognition by conformational selection. FEBS Lett. 450, 149–53 (1999).
Dürr, E., Jelesarov, I. & Bosshard, H. R. Extremely fast folding of a very stable leucine zipper with a strengthened hydrophobic core and lacking electrostatic interactions between helices. Biochemistry 38, 870–80 (1999).
Jelesarov, I. & Bosshard, H. R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 12, 3–18 (1999).
Berger, C., Piubelli, L., Haditsch, U. & Bosshard, H. R. Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor. FEBS Lett. 425, 14–8 (1998).
Hanes, J., Jermutus, L., Weber-Bornhauser, S., Bosshard, H. R. & Plückthun, A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc. Natl. Acad. Sci. U. S. A. 95, 14130–5 (1998).
Jelesarov, I., Dürr, E., Thomas, R. M. & Bosshard, H. R. Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper). Biochemistry 37, 7539–50 (1998).
Weber-Bornhauser, S., Eggenberger, J., Jelesarov, I., Bernard, A., Berger, C. & Bosshard, H. R. Thermodynamics and kinetics of the reaction of a single-chain antibody fragment (scFv) with the leucine zipper domain of transcription factor GCN4. Biochemistry 37, 13011–20 (1998).
Dürr, E. & Bosshard, H. R. A monoclonal antibody induces opening of a coiled coil. Global protection of amide protons from H/D exchange decreases by up to 1000-fold in antibody-bound triple-stranded coiled coil. Eur. J. Biochem. 249, 325–9 (1997).
Krebber, A., Bornhauser, S., Burmester, J., Honegger, A., Willuda, J., Bosshard, H. R. & Plückthun, A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods 201, 35–55 (1997).
Piubelli, L., Zanetti, G. & Bosshard, H. R. Recombinant wild-type and mutant complexes of ferredoxin and ferredoxin:NADP+ reductase studied by isothermal titration calorimetry. Biol. Chem. 378, 715–8 (1997).
Wendt, H., Leder, L., Harma, H., Jelesarov, I., Baici, A. & Bosshard, H. R. Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry 36, 204–13 (1997).
Berger, C., Jelesarov, I. & Bosshard, H. R. Coupled folding and site-specific binding of the GCN4-bZIP transcription factor to the AP-1 and ATF/CREB DNA sites studied by microcalorimetry. Biochemistry 35, 14984–91 (1996).
Bosshard, H. R. Epitope mapping by differential chemical modification of antigens. Methods Mol. Biol. 66, 85–95 (1996).
Jelesarov, I. & Bosshard, H. R. Thermodynamic characterization of the coupled folding and association of heterodimeric coiled coils (leucine zippers). J. Mol. Biol. 263, 344–58 (1996).
Jelesarov, I. I., Leder, L. & Bosshard, H. R. Probing the Energetics of Antigen-Antibody Recognition by Titration Microcalorimetry. Methods 9, 533–41 (1996).
Bernard, A. & Bosshard, H. R. Real-time monitoring of antigen-antibody recognition on a metal oxide surface by an optical grating coupler sensor. Eur. J. Biochem. 230, 416–23 (1995).
Leder, L., Berger, C., Bornhauser, S., Wendt, H., Ackermann, F., Jelesarov, I. & Bosshard, H. R. Spectroscopic, calorimetric, and kinetic demonstration of conformational adaptation in peptide-antibody recognition. Biochemistry 34, 16509–18 (1995).
Przybylski, M., Kast, J., Glocker, M. O., Dürr, E., Bosshard, H. R., Nock, S. & Sprinzl, M. Mass spectrometric approaches to molecular characterization of protein-nucleic acid interactions. Toxicol Lett. 82–83, 567–75 (1995).
Wendt, H., Berger, C., Baici, A., Thomas, R. M. & Bosshard, H. R. Kinetics of folding of leucine zipper domains. Biochemistry 34, 4097–107 (1995).
Wendt, H., Dürr, E., Thomas, R. M., Przybylski, M. & Bosshard, H. R. Characterization of leucine zipper complexes by electrospray ionization mass spectrometry. Protein Sci. 4, 1563–70 (1995).
De Pascalis, A. R., Schurmann, P. & Bosshard, H. R. Comparison of the binding sites of plant ferredoxin for two ferredoxin-dependent enzymes. FEBS Lett. 337, 217–20 (1994).
Jelesarov, I. & Bosshard, H. R. Thermodynamics of ferredoxin binding to ferredoxin:NADP+ reductase and the role of water at the complex interface. Biochemistry 33, 13321–8 (1994).
Leder, L. & Bosshard, H. R. Immunoreactivity of cytochrome c: antibodies to horse cytochrome c distinguish between sequence-related cytochromes only at the level of the 3-D-structure. Biochimie 76, 465–70 (1994).
Leder, L., Wendt, H., Schwab, C., Jelesarov, I., Bornhauser, S., Ackermann, F. & Bosshard, H. R. Genuine and apparent cross-reaction of polyclonal antibodies to proteins and peptides. Eur. J. Biochem. 219, 73–81 (1994).
De Pascalis, A. R., Jelesarov, I., Ackermann, F., Koppenol, W. H., Hirasawa, M., Knaff, D. B. & Bosshard, H. R. Binding of ferredoxin to ferredoxin:NADP+ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment. Protein Sci. 2, 1126–35 (1993).
Jelesarov, I., De Pascalis, A. R., Koppenol, W. H., Hirasawa, M., Knaff, D. B. & Bosshard, H. R. Ferredoxin binding site on ferredoxin: NADP+ reductase. Differential chemical modification of free and ferredoxin-bound enzyme. Eur. J. Biochem. 216, 57–66 (1993).
Ngai, P. K., Ackermann, F., Wendt, H., Savoca, R. & Bosshard, H. R. Protein A antibody-capture ELISA (PACE): an ELISA format to avoid denaturation of surface-adsorbed antigens. J. Immunol. Methods 158, 267–76 (1993).
Schwab, C., Twardek, A., Lo, T. P., Brayer, G. D. & Bosshard, H. R. Mapping antibody binding sites on cytochrome c with synthetic peptides: are results representative of the antigenic structure of proteins? Protein Sci. 2, 175–82 (1993).
Schwab, C. & Bosshard, H. R. Caveats for the use of surface-adsorbed protein antigen to test the specificity of antibodies. J. Immunol. Methods 147, 125–34 (1992).
Savoca, R., Schwab, C. & Bosshard, H. R. Epitope mapping employing immobilized synthetic peptides. How specific is the reactivity of these peptides with antiserum raised against the parent protein? J. Immunol. Methods 141, 245–52 (1991).
Schweizer, M., Peter, M. A., Filipovic, D., Tinner, R., Bosshard, H. R. & Oertle, M. Mechanism of monoclonal antibody inhibition/stimulation of reactions catalyzed by cytochrome P450IIB1. Arch. Biochem. Biophys. 288, 64–70 (1991).
Saad, B. & Bosshard, H. R. Antigenic sites on cytochrome c2 from Rhodospirillum rubrum. Eur. J. Biochem. 187, 425–30 (1990).
Tinner, R., Oertle, M., Heizmann, C. W. & Bosshard, H. R. Ca2(+)-binding site of carp parvalbumin recognized by monoclonal antibody. Cell Calcium 11, 19–23 (1990).
Michel, B. & Bosshard, H. R. Oxidation of cytochrome c by cytochrome c oxidase: spectroscopic binding studies and steady-state kinetics support a conformational transition mechanism. Biochemistry 28, 244–52 (1989).
Michel, B., Mauk, A. G. & Bosshard, H. R. Binding and oxidation of mutant cytochromes c by cytochrome-c oxidase. FEBS Lett. 243, 149–52 (1989).
Michel, B., Proudfoot, A. E., Wallace, C. J. & Bosshard, H. R. The cytochrome c oxidase-cytochrome c complex: spectroscopic analysis of conformational changes in the protein-protein interaction domain. Biochemistry 28, 456–62 (1989).
Oertle, M., Immergluck, K., Paterson, Y. & Bosshard, H. R. Mapping of four discontiguous antigenic determinants on horse cytochrome c. Eur. J. Biochem. 182, 699–704 (1989).
Ritzmann, M. & Bosshard, H. R. Sulfite oxidase from chicken liver. Further characterization of the role of carboxyl groups in the reaction with cytochrome c. Eur. J. Biochem. 172, 377–81 (1988).
Saad, B., Corradin, G. & Bosshard, H. R. Monoclonal antibody recognizes a conformational epitope in a random coil protein. Eur. J. Biochem. 178, 219–24 (1988).
Bosshard, H. R., Snozzi, M. & Bachofen, R. Interaction of horse cytochrome c with the photosynthetic reaction center of Rhodospirillum rubrum. J. Bioenerg. Biomembr. 19, 375–82 (1987).
Burnens, A., Demotz, S., Corradin, G., Binz, H. & Bosshard, H. R. Epitope mapping by chemical modification of free and antibody-bound protein antigen. Science 235, 780–3 (1987).
Weber, C., Michel, B. & Bosshard, H. R. Spectroscopic analysis of the cytochrome c oxidase-cytochrome c complex: circular dichroism and magnetic circular dichroism measurements reveal change of cytochrome c heme geometry imposed by complex formation. Proc. Natl. Acad. Sci. U. S. A. 84, 6687–91 (1987).
Bosshard, H. R., Davidson, M. W., Knaff, D. B. & Millett, F. Complex formation and electron transfer between mitochondrial cytochrome c and flavocytochrome c552 from Chromatium vinosum. J. Biol. Chem. 261, 190–3 (1986).
Ritzmann, M. & Bosshard, H. R. Sulfite oxidase from chicken liver. The role of imidazole and carboxyl groups for the reaction with cytochrome c. Eur. J. Biochem. 159, 493–7 (1986).
Bechtold, R. & Bosshard, H. R. Structure of an electron transfer complex. II. Chemical modification of carboxyl groups of cytochrome c peroxidase in presence and absence of cytochrome c. J. Biol. Chem. 260, 5191–200 (1985).
Rieder, R., Wiemken, V., Bachofen, R. & Bosshard, H. R. Binding of cytochrome c2 to the isolated reaction center of Rhodospirillum rubrum involves the "backside" of cytochrome c2. Biochem. Biophys. Res. Commun. 128, 120–6 (1985).
Waldmeyer, B. & Bosshard, H. R. Structure of an electron transfer complex. I. Covalent cross-linking of cytochrome c peroxidase and cytochrome c. J. Biol. Chem. 260, 5184–90 (1985).
Bosshard, H. R. [Cytochrome c function--a model of molecular recognition]. Postepy Biochem. 30, 225–30 (1984).
Bosshard, H. R., Bänziger, J., Hasler, T. & Poulos, T. L. The cytochrome c peroxidase-cytochrome c electron transfer complex. The role of histidine residues. J. Biol. Chem. 259, 5683–90 (1984).
Michel, B. & Bosshard, H. R. Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. J. Biol. Chem. 259, 10085–91 (1984).
Waldmeyer, B., Bechtold, R., Bosshard, H. R. & Poulos, T. L. The cytochrome c peroxidase.cytochrome c electron transfer complex. Experimental support of a hypothetical model. J. Biol. Chem. 257, 6073–6 (1982).
Bosshard, H. R. Alkaline isomerization of ferricytochrome c: lysine is not replacing methionine at the sixth co-ordination site of the haem iron. J. Mol. Biol. 153, 1125–49 (1981).
Bosshard, H. R. & Zurrer, M. The conformation of cytochrome c in solution. Localization of a conformational difference between ferri- and ferrocytochrome c on the surface of the molecule. J. Biol. Chem. 255, 6694–9 (1980).
Rieder, R. & Bosshard, H. R. Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c. J. Biol. Chem. 255, 4732–9 (1980).
Waldmeyer, B., Bechtold, R., Zurrer, M. & Bosshard, H. R. Crosslinking of cytochrome c to peroxidase: covalent complex catalyzes oxidation of cytochrome c1 by H2O2. FEBS Lett. 119, 349–51 (1980).
Bosshard, H. R. Mapping of contact areas in protein-nucleic acid and protein-protein complexes by differential chemical modification. Methods Biochem. Anal. 25, 273–301 (1979).
Bosshard, H. R., Zurrer, M., Schagger, H. & von Jagow, G. Binding of cytochrome c to the cytochrome bc1 complex (complex III) and its subunits cytochrome c1 and b1. Biochem. Biophys. Res. Commun. 89, 250–8 (1979).
Bosshard, H. R., Koch, G. L. & Harley, B. S. The aminoacyl-tRNA synthetase-tRNA complex: detection by differential labelling of lysine residues involved in complex formation. J. Mol. Biol. 119, 377–89 (1978).
Rieder, R. & Bosshard, H. R. The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome c. J. Biol. Chem. 253, 6045–53 (1978).
Rieder, R. & Bosshard, H. R. Cytochrome bc1 and cytochrome oxidase can bind to the same surface domain of the cytochrome c molecule. FEBS Lett. 92, 223–6 (1978).
Bosshard, H. R. Theories of enzyme specificity and their application to proteases and aminoacyl-transfer RNA synthetases. Experientia 32, 949–63 (1976).
Bosshard, H. R., Koch, L. E. & Hartley, B. S. Aminoacyl-tRNA synthetases from Bacillus stearothermophilus. Asymmetry of substrate binding to tyrosyl-tRNA synthetase. Eur. J. Biochem. 53, 493–8 (1975).
Bosshard, H. R. & Berger, A. The topographical differences in the active site region of alpha-chymotrypsin, subtilisin Novo, and subtilisin Carlsberg. Mapping the aromatic binding site by inhibitors (virtual substrates). Biochemistry 13, 266–77 (1974).
Rampini, S., Vollmin, J. A., Bosshard, H. R., Muller, M. & Curtius, H. C. Aromatic acids in urine of healthy infants, persistent hyperphenylalaninemia, and phenylketonuria, before and after phenylalanine load. Pediatr. Res. 8, 704–9 (1974).
Berger, A., Smolarsky, M., Kurn, N. & Bosshard, H. R. A new method for the synthesis of optically active -amino acids and their N derivatives via acylamino malonates. J. Org. Chem. 38, 457–60 (1973).
Bosshard, H. R. Kinetic evidence for two different productive substrate binding sites in subtilisins. FEBS Lett. 30, 105–110 (1973).
Bosshard, H. R., Schechter, I. & Berger, A. A new method for the detection of racemization during peptide synthesis: stereoselective hydrolysis of diastereomeric peptides by leucine aminopeptidase. Helv. Chim. Acta 56, 717–23 (1973).
Bosshard, H. R. [Synthesis of new derivatives of insulin sequence B1-8 with improved solubility]. Helv. Chim. Acta 54, 951–8 (1971).
Bünzli, H. F. & Bosshard, H. R. Modification of the single arginine residue in insulin with phenylglyoxal. Hoppe Seylers Z. Physiol. Chem. 352, 1180–2 (1971).
Vollmin, J. A., Bosshard, H. R., Muller, M., Rampini, S. & Curtius, H. C. Determination of urinary aromatic acids by gas chromatography. Results from healthy infants and from patients with phenylketonuria. Z. Klin. Chem. Klin. Biochem. 9, 402–4 (1971).
Pioda, L. A., Simon, W., Bosshard, H. R. & Curtius, C. H. Determination of potassium ion concentration in serum using a highly selective liquid-membrane electrode. Clin. Chim. Acta 29, 289–93 (1970).
Bosshard, H. R., Jorgensen, K. H. & Humbel, R. E. Preparation and properties of cyanoethylated insulin. An insulin derivative with blocked amino- and imidazole-groups. Eur. J. Biochem. 9, 353–62 (1969).
