Publications

1.: Wüthrich, K. und Fallab, S. (1963) Chimia 17, 356-358.
Bestimmung der Bildungskonstanten der o-Phenylendiamin-Kupfer(II)-Komplexe in wässriger Lösung.
2.: Wüthrich, K. und Fallab, S. (1964) Helv. Chim. Acta 47, 1440-1448.
Mechanismus der Kupfer(II)-katalysierten Autoxydation von o-Phenylendiamin.
3.: Wüthrich, K. und Fallab, S. (1964) Helv. Chim. Acta 47, 1609-1616.
Einfluss verschiedener Liganden auf den Mechanismus der Kupfer(II)-katalysierten Autoxydation von o-Phenylendiamin.
4.: Wüthrich, K., Loeliger, H. und Fallab, S. (1964) Experientia 20, 599-601.
Elektronenspinresonanzmessungen zur Untersuchung von Kinetik und Mechanismus von Cu2+-katalysierten Reaktionen.
5.: Wüthrich, K. (1965) Helv. Chim. Acta 48, 779-790.
Elektronenspinresonanz-Untersuchungen von VO2+-Komplexverbindungen in wässeriger Lösung.
6.: Wüthrich, K. (1965) Helv. Chim. Acta 48, 1012-1017.
Elektronenspinresonanz-Untersuchungen von VO2+-Komplexverbindungen in wässeriger Lösung II.
7.: Wüthrich, K. (1966) Helv. Chim. Acta 49, 1400-1406.
Über die Elektronenspinresonanzspektren einiger Cu2+-Komplexe in wässeriger Lösung.
8.: Wüthrich, K. and Connick, R.E. (1967) Inorg. Chem. 6, 583-590.
Nuclear magnetic resonance relaxation of oxygen-17 in aqueous solutions of vanadyl perchlorate and the rate of elimination of water molecules from the first coordination sphere.
9.: Wüthrich, K., Shulman, R.G. and Peisach, J. (1968) Proc. Natl. Acad. Sci. USA 60,
373-380.
High resolution proton magnetic resonance spectra of sperm whale cyanometmyoglobin.
10.: Wüthrich, K. and Connick, R.E. (1968) Inorg. Chem. 7, 1377-1388.
Nuclear magnetic resonance studies of the coordination of vanadyl complexes in solution and the rate of elimination of coordinated water molecules.
11.: Wüthrich, K., Shulman, R.G. and Yamane, T. (1968) Proc. Natl. Acad. Sci. USA 61,
1199-206.
Proton magnetic resonance studies of human cyanomethemoglobin.
12.: Wüthrich, K., Shulman, R.G., Wyluda, B.J. and Caughey, W.S. (1969) Proc. Natl. Acad. Sci. USA 62, 636-643.
Proton magnetic resonance studies of porphyrin iron(III) cyanides.
13.: Shulman, R.G., Ogawa, S., Wüthrich, K., Yamane, T., Peisach, J. and Blumberg, W.E. (1969) Science 165, 251-257.
The absence of ``heme-heme'' interactions in hemoglobin.
14.: Shulman, R.G., Wüthrich, Yamane, T., Antonini, E. and Brunori, M. (1969) Proc. Natl. Acad. Sci. USA 63, 623-628.
Nuclear magnetic resonances of reconstituted myoglobins.
15.: Wüthrich, K. (1969) Proc. Natl. Acad. Sci. USA 63, 1071-1078.
High resolution proton nuclear magnetic resonance spectroscopy of cytochrome c.
16.: Connick, R.E. and Wüthrich, K. (1969) J. Chem. Phys. 51, 4506-4508.
17O nuclear magnetic relaxation in aqueous solutions of diamagnetic metal ions.
17.: Wüthrich, K., Meiboom, S. and Snyder, L.C. (1970) J. Chem. Phys. 52, 230-233.
Nuclear magnetic resonance spectroscopy of bicyclobutane.
18.: Wüthrich, K. and Shulman, R.G. (1970) Physics Today 23, 43-50.
Magnetic resonance in biology.
19.: Yamane, T., Wüthrich, K., Shulman, R.G. and Ogawa, S. (1970) J. Mol. Biol. 49, 197-202.
Proton magnetic resonance studies of cyanoferrihemoglobins from different species.
20.: Wüthrich, K., Shulman, R.G., Yamane, T., Wyluda, B.J., Hügli , B.J. and Gurd, F.R.N. (1970) J. Biol. Chem. 245, 1947-1953.
High resolution proton magnetic resonance studies of cyanoferrimyoglobins and alkylated derivatives from different species.
21.: Shulman, R.G., Wüthrich, K., Yamane, T., Patel, D.J. and Blumberg, W.E. (1970) J. Mol. Biol. 53, 143-157.
Nuclear magnetic resonance determination of ligand-induced conformational changes in myoglobin.
22.: Wüthrich, K. (1970) Structure and Bonding 8, 53-121.
Structural studies of hemes and hemoproteins by nuclear magnetic resonance spectroscopy.
23.: Wüthrich, K. (1970) Chimia 24, 409-418.
Studien der räumlichen Struktur von Proteinmolekülen mit magnetischer Kernresonanzspektroskopie.
24.: Shulman, R.G., Ogawa, S., Wüthrich, K., Yamane, T., Peisach, J. and Blumberg, W.E. (1970) in Physical Problems in Biological Systems, (C. de Witt and J. Matricon, eds.)
pp. 235-249, Gordon and Breach, New York.
The absence of ``heme-heme'' interactions in hemoglobin.
25.: Wüthrich, K. (1970) dans Physique et Chimie, Numéro Spécial Annuel 1970: La Biophysique, pp. 18-25, Editions de l'Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris.
Structures électroniques dans les hémoprotéines: études par résonance magnétique nucléaire.
26.: Wüthrich, K., Meraldi, J.P., Tun-Kyi, A. and Schwyzer, R. (1971) in Proc. 1st Eur. Biophysics Congress, Vol. I, pp. 93-95, Verlag der Wiener Medizinischen Akademie.
Structural studies by nuclear magnetic resonance of a cationspecific peptide.
27.: Shulman, R.G., Wüthrich, K. and Peisach, J. (1971) in Probes of Structure and Function of Macromolecules and Membranes, Vol. II: Probes of Enzymes and Hemoproteins (B. Chance, T. Yonetani and A.S. Mildvan, eds.) pp. 195-204, Academic Press, New York.
High resolution proton magnetic resonance studies of myoglobin.
28.: Wüthrich, K. (1971) in Probes of Structure and Function of Macromolecules and Membranes, Vol. II: Probes of Enzymes and Hemoproteins (B. Chance, T. Yonetani and A.S. Mildvan, eds.) pp. 465-486, Academic Press, New York.
High resolution proton NMR studies of the coordination of the heme iron in cytochrome c.
29.: Wüthrich, K., Aviram, I. and Schejter, A. (1971) Biochim. Biophys. Acta 253, 98-103.
Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy.
30.: Ogawa, S., Shulman, R.G., Wüthrich, K. and Yamane, T. (1971) in Magnetic Resonances in Biological Research (C. Franconi, ed.) pp. 97-106, Gordon and Breach, New York.
NMR studies of the role of the heme group during the cooperative oxygenation of hemoglobin.
31.: Wüthrich, K., Shulman, R.G., Yamane, T. and Ogawa, S. (1971) in Genetical, Functional and Physical Studies of Hemoglobins (T. Arends, G. Bemski and R.L. Nagel, eds.)
pp. 73-79, Karger, Basel.
Studies of structure-function correlations in hemoglobin by nuclear magnetic resonance.
32.: Winterhalter, K.H. and Wüthrich, K. (1972) J. Mol. Biol. 63, 477-482.
Structural investigations of modified haemoglobins by nuclear magnetic resonance spectroscopy.
33.: Keller, R.M., Aviram, I., Schejter, A. and Wüthrich, K. (1972) FEBS Lett. 20, 90-92.
Evidence for pentacoordinated iron (II) in carboxymethylated cytochrome c.
34.: Wüthrich, K. and Shulman, R.G. (1971) Uspekhi Fizicheskikh Nauk 105, 707-720.
Magnetic resonance in biology. (Russisch)
35.: Wüthrich, K., Keller, R.M., Brunori, M., Giacometti, G., Huber, R. and Formanek, H. (1972) FEBS Lett. 21, 63-66.
Similarities of the heme environment in vertebrate and non-vertebrate oxygen-binding hemoproteins.
36.: Donzel, B., Kamber, B., Wüthrich, K. and Schwyzer, R. (1972) Helv. Chim. Acta 55,
947-961.
A chiral cystine disulfide group without inherent optical activity in the long-wavelength region.
37.: Keller, R.M., Wüthrich, K. and Debrunner, P.G. (1972) Proc. Natl. Acad. Sci. USA 69, 2073-2075 .
Proton magnetic resonance reveals high spin iron (II) in ferrous cytochrome P450cam from Pseudomonas putida.
38.: Wüthrich, K., Tun-Kyi , A. and Schwyzer, R. (1972) FEBS Lett. 25, 104-108.
Manifestation in the 13C NMR spectra of two different molecular conformations of a cyclic pentapeptide.
39.: Meraldi, J.P., Schwyzer, R., Tun-Kyi, A. and Wüthrich, K. (1972) Helv. Chim. Acta 55, 1962-1973.
Conformational studies of cyclic pentapeptides by proton magnetic resonance spectroscopy.
40.: Schwyzer, R., Grathwohl, C., Meraldi, J.P., Tun-Kyi, A., Vogel, R. and Wüthrich, K. (1972) Helv. Chim. Acta 55, 2545-2549.
The solution conformation of cyclo-glycyl-L-prolyl-glycyl-glycyl-L-prolyl-glycyl.
41.: Keller, R.M. and Wüthrich, K. (1972) Biochim. Biophys. Acta 285, 326-336.
The electronic g-tensor in cytochrome b5 : high resolution proton magnetic resonance studies.
42.: Grathwohl, C., Schwyzer, R., Tun-Kyi, A. and Wüthrich, K. (1973) FEBS Lett. 29,
271-274.
Carbon-13 NMR spectra of cyclo-glycyl-L-prolyl-glycyl-glycyl-L-prolyl- glycyl: assignment of the carbonyl resonances.
43.: Wüthrich, K. (1973) in Vorträge des 9. Kolloquiums über NMR-Spektroskopie (R. Kosfeld, J. Mansfeld und P. Puhr-Westerheide, eds.) Vol. 1, pp. 71-91, Rheinisch-Westfälische Technische Hochschule Aachen.
Proton and carbon-13 NMR studies of peptides and proteins.
44.: Masson, A. and Wüthrich, K. (1973) FEBS Lett. 31, 114-118.
Proton magnetic resonance investigation of the conformational properties of the basic pancreatic trypsin inhibitor.
45.: Wüthrich, K. and Baumann, R. (1973) Helv. Chim. Acta 56, 585-596.
Hyperfine shifts of the 13C NMR in low spin iron(III) porphyrin complexes.
46.: Wüthrich, K. (1973) Naturwissenschaften 60, 221-230.
Magnetische Kernresonanzspektroskopie in der Biologischen Forschung.
47.: Keller, R.M., Pettigrew, G.W. and Wüthrich, K. (1973) FEBS Lett. 36, 151-156.
Structural studies by proton NMR of cytochrome c-557 from Crithidia oncopelti.
48.: Keller, R.M., Groudinsky, O. and Wüthrich, K. (1973) Biochim. Biophys. Acta 328,
233-238.
Proton magnetic resonances in cytochrome b2 core: structural similarities with cytochrome b5.
49.: Wüthrich, K., Keller, R.M. and Baumann, R. (1973) in Dynamic Aspects of Conformation Changes in Biological Macromolecules (C. Sadron, ed.) pp. 151-163. Reidel, Dordrecht.
Proton and carbon-13 nuclear magnetic resonances in hemes and hemoproteins: new aspects for the investigation of the molecular conformations.
50.: Meraldi, J.P., Moeschler, H., Schwyzer, R., Tun-Kyi, A. et Wüthrich, K. (1973) J. Physique 34, C8-41 - C8-43.
Etudes de la conformation de pentapeptides cycliques par la résonance magnétique nucléaire.
51.: Wüthrich, K. and Baumann, R. (1973) Ann. New York Acad. Sci 222, 709-721 (1973).
Recent developments in the investigation of the paramagnetic centers in low spin ferric hemoproteins: carbon-13 hyperfine shifts in iron porphyrin complexes.
52.: Wüthrich, K. and Baumann, R. (1974) Helv. Chim. Acta 57, 336-350.
Hyperfine shifts of the 13C NMR in protoporphyrin IX iron(III) dicyanide and deuteroporphyrin IX iron(III) dicyanide.
53.: Grathwohl , C. and Wüthrich, K. (1974) J. Magn. Reson. 13, 217-225.
Carbon-13 NMR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala- OCH3, where X stands for the 20 common amino acids.
54.: Wüthrich, K. (1974) Experientia 30, 577-585.
Nuclear magnetic resonance in protein research.
55.: Wüthrich, K. (1974) Pure Appl.Chem. 37, 235-248.
Studies of the molecular conformations in proteins by 1H and 13C NMR spectroscopy.
56.: Wüthrich, K. and Grathwohl, C. (1974) FEBS Lett. 43, 337-340.
A novel approach for studies of the molecular conformations in flexible polypeptides.
57.: Wüthrich, K. and Keller, R.M. (1973) in Symposial Papers of the IVth International Biophysics Congress, Vol. 2, pp. 722-735, Academy of Sciences of the USSR, Pushino.
Recent developments in the investigation of the paramagnetic centers in low spin ferric hemoproteins.
58.: Wüthrich, K., Grathwohl, C. and Schwyzer, R. (1974) in Peptides, Polypeptides and Proteins (E.R. Blout, F.A. Bovey, M. Goodman and N. Lotan, eds.) pp. 300-307, Wiley, New York.
Cis, trans, and nonplanar peptide bonds in oligopeptides: 13C NMR studies.
59.: Wüthrich, K. (1974) Pure Appl. Chem. 40, 127-139.
Carbon-13 NMR in haems and haemoproteins.
60.: Grathwohl, C., Tun-Kyi, A., Bundi, A., Schwyzer, R. and Wüthrich, K. (1975) Helv. Chim. Acta 58, 415-423 .
1H and 13C NMR studies of the molecular conformations of cyclo-tetraglycyl.
61.: Wüthrich, K. and Wagner, G. (1975) FEBS Lett. 50, 265-268.
NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor.
62.: Bundi, A., Grathwohl, C., Hochmann, J., Keller, R.M., Wagner, G. and Wüthrich, K. (1975) J. Magn. Reson. 18, 191-198.
Proton NMR of the protected tetrapeptides TFA-Gly-Gly-L-X-L-Ala-OCH3, where X stands for one of the 20 common amino acids.
63.: Wüthrich, K., Hochmann, J., Keller, R.M., Wagner, G., Brunori, M. and Giacometti, G.
J. Magn. Reson. 19, 111-113 (1975).
1H NMR relaxation in high spin ferrous hemoproteins.
64.: Llinás, M., Wüthrich, K., Schwotzer, W. and von Philipsborn, W. (1975) Nature 257, 817-818.
15N nuclear magnetic resonance of living cells.
65.: Wüthrich, K. (1975) in Proc. 10th FEBS Meeting, pp. 21-24, Federation of European Biochemical Societies.
Nuclear magnetic resonance in enzyme research.
66.: Wagner, G. and Wüthrich, K. (1975) J. Magn. Reson. 20, 435-445.
Proton NMR studies of the aromatic residues in the basic pancreatic trypsin inhibitor (BPTI).
67.: Wagner, G., DeMarco, A. and Wüthrich, K. (1975) J. Magn. Reson. 20, 565-569.
Convolution difference 1H NMR spectra at 360 MHz of the basic pancreatic trypsin inhibitor.
68.: Brown, L.R., DeMarco, A., Wagner, G. and Wüthrich, K. (1976) Eur. J. Biochem. 62, 103-107.
A study of the lysyl residues in the basic pancreatic trypsin inhibitor using 1H nuclear magnetic resonance at 360 MHz.
69.: Wüthrich, K. (1976) NMR in Biological Research: Peptides and Proteins, 379 pages. North Holland, Amsterdam.
70.: Wagner, G. and Wüthrich, K. (1976) in Protides of the Biological Fluids - 23rd Colloquium (H. Peeters, ed.) pp. 189-193, Pergamon, Oxford.
1H NMR studies of the dynamics of the solution conformation of the basic pancreatic trypsin inhibitor (BPTI).
71.: Wüthrich, K., Wagner, G. and Tschesche, H. (1976) in Protides of the Biological Fluids-23rd Colloquium (H. Peeters, ed.) pp. 201-204, Pergamon, Oxford.
Comparative 1H NMR studies of the solution conformation of the cow colostrum trypsin inhibitor (CTI), the trypsin inhibitor of helix pomatia (HPI) and the basic pancreatic trypsin inhibitor (BPTI).
72.: Keller, R.M., Groudinsky, O. and Wüthrich, K. (1976) Biochim. Biophys. Acta 427, 497-511.
Contact-shifted resonances in the 1H NMR spectra of cytochrome b5: resonance identification and spin density distribution in the heme group.
73.: Bundi, A., Andreatta, R., Rittel, W. and Wüthrich, K. (1976) FEBS Lett. 64, 126-129.
Conformational studies of the synthetic fragment 1-34 of human parathyroid hormone by NMR techniques.
74.: Wagner, G., DeMarco, A. and Wüthrich, K. (1976) Biophys. Struct. Mech. 2, 139-158.
Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) I: 1H NMR studies.
75.: Hetzel, R., Wüthrich, K., Deisenhofer, J. and Huber, R. (1976) Biophys. Struct. Mech. 2, 159-180.
Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI) II: semi-empirical energy calculations.
76.: Wüthrich, K. (1975) in Metalloprotein Studies Utilizing Paramagnetic Effects of the Metal Ions as Probes (M. Kotani and A. Tasaki, eds.) pp. 151-179, The Taniguchi Foundation, Osaka, Japan.
The heme groups as natural NMR probes of hemoprotein conformation.
77.: Möschler, H.J., Tun-Kyi, A., Meraldi, J.P., Wüthrich, K. und Schwyzer, R. (1976) Helv. Chim. Acta 59, 2196-2200.
Synthese deuterierter Derivate diastereomerer Cyclopentapeptide für die Konformationsanalyse.
78.: Wüthrich, K. and DeMarco, A. (1976) Helv. Chim. Acta 59, 2228-2235.
Preferred spatial arrangement of the aromatic side chains in linear oligopeptides containing tyrosine.
79.: Grathwohl, C. and Wüthrich, K. (1976) Biopolymers 15, 2025-2041.
The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides.
80.: Grathwohl, C. and Wüthrich, K. (1976) Biopolymers 15, 2043-2057.
NMR studies of the molecular conformations in the linear oligopeptides
H-(L-Ala)n-L-Pro-OH.
81.: Keller, R.M., Wüthrich, K. and Pecht, I. (1976) FEBS Lett. 70, 180-184.
Structural studies of cytochrome c-551 by 1H NMR spectroscopy at 360 MHz.
82.: DeMarco, A. and Wüthrich, K. (1976) J. Magn. Reson. 24, 201-204.
Digital filtering with a sinusoidal window function: an alternative technique for resolution enhancement in FT NMR.
83.: Wüthrich, K. and Baumann, R. (1976) Org. Magn. Reson. 8, 532-535.
13C spin relaxation studies of the basic pancreatic trypsin inhibitor.
84.: Brown, L.R. and Wüthrich, K. (1977) Biochim. Biophys. Acta 464, 356-369.
A spin label study of lipid oxidation catalyzed by heme proteins.
85.: Keller, R.M., Wüthrich, K. and Schejter, A. (1977) Biochim. Biophys. Acta 491, 409-415.
1H NMR studies of the heme iron coordination in cytochrome c-552 from Euglena gracilis.
86.: Keller, R.M. and Wüthrich, K. (1977) Biochim. Biophys. Acta 491, 416-422.
1H NMR studies at 360 MHz of the aromatic amino acid residues in ferrocytochrome
c-552 from Euglena gracilis.
87.: Bundi, A. and Wüthrich, K. (1977) FEBS Lett. 77, 11-14.
1H NMR titration shifts of amide proton resonances in polypeptide chains.
88.: Llinás, M., Meier, W. and Wüthrich, K. (1977) Biochim. Biophys. Acta 492, 1-11.
A carbon-13 spin lattice relaxation study of alumichrome at 25.1 MHz and 90.5 MHz.
89.: Lauterwein, J., Wüthrich, K., Schweitz, H., Vincent, J.P. and Lazdunski, M. (1977) Biochem. Biophys. Res. Comm. 76, 1071-1078.
1H NMR studies of a neurotoxin and a cardiotoxin from Naja mossambica mossambica: amide proton resonances.
90.: Richarz, R. and Wüthrich, K. (1977) FEBS Lett. 79, 64-68.
High field 13C NMR studies at 90.5 MHz of the methyl groups in the basic pancreatic trypsin inhibitor.
91.: Brown, L.R. and Wüthrich, K. (1977) Biochim. Biophys. Acta 468, 389-410.
NMR and ESR studies of the interactions of cytochrome c with mixed cardiolipin phosphatidylcholine vesicles.
92.: Wüthrich, K. (1977) in Nuclear Magnetic Resonance in Solids (L. van Gerven, ed.)
pp. 347-360, Plenum Press, New York.
NMR studies of structure and conformation in peptides and proteins.
93.: Wüthrich, K. (1977) in Nuclear Magnetic Resonance in Solids (L. van Gerven, ed.) pp. 361-374, Plenum Press, New York.
NMR studies of hemoproteins.
94.: Wüthrich, K., Wagner, G., Richarz, R. and DeMarco, A. (1977) in NMR in Biology, (R.A. Dwek, I.D. Campbell, R.E. Richards and R.J.P. Williams, eds.) pp. 51-62, Academic Press, New York.
Completion of X-ray structures of proteins by high resolution NMR.
95.: DeMarco, A., Tschesche, H., Wagner, G. and Wüthrich, K. (1977) Biophys. Struct. Mech. 3,
303-315.
1H NMR studies at 360 MHz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI).
96.: Nagayama, K., Wüthrich, K., Bachmann, P. and Ernst, R.R. (1977) Biochem. Biophys. Res. Comm. 78, 99-105.
Two-dimensional J-resolved 1H NMR spectroscopy of biological macromolecules.
97.: Nagayama, K., Wüthrich, K., Bachmann, P. and Ernst, R.R. (1977) Naturwissenschaften 64, 581-582.
Two-dimensional NMR spectroscopy: a powerful tool for the investigation of biopolymers in solution.
98.: Llinás, M. and Wüthrich, K. (1978) Biochim. Biophys. Acta 532, 29-40.
A nitrogen-15 spin-lattice relaxation study of alumichrome.
99.: Keller, R.M. and Wüthrich, K. (1978) Biochim. Biophys. Acta 533, 195-208.
Assignment of the heme c resonances in the 360 MHz 1H NMR spectra of cytochrome c.
100.: DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 617-636.
Analysis of the 1H NMR spectra of ferrichrome peptides I: the non-amide protons.
101.: DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 637-650.
Analysis of the 1H NMR spectra of ferrichrome peptides II: the amide resonances.
102.: Wagner, G., Wüthrich, K. and Tschesche, H. (1978) Eur. J. Biochem. 86, 67-76.
A 1H nuclear magnetic resonance study of the conformation and the molecular dynamics of the glycoprotein cow colostrum trypsin inhibitor.
103.: Richarz, R. and Wüthrich, K. (1978) J. Magn. Reson. 30, 147-150.
NOE difference spectroscopy: a novel method for observing individual multiplets in proton nmr spectra of biological macromolecules.
104.: Brown, L.R., DeMarco, A., Richarz, R., Wagner, G. and Wüthrich, K. (1978) Eur. J. Biochem. 88, 87-95.
The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor: 1H and 13C nuclear magnetic resonance studies of the native and the transaminated inhibitor.
105.: Wüthrich, K., Wagner, G., Richarz, R. and Perkins, S.J. (1978) Biochemistry 17,
2253-2263.
Individual assignments of the methyl resonances in the 1H nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor.
106.: Richarz, R. and Wüthrich, K. (1978) Biochemistry 17, 2263-2269 .
High field 13C nuclear magnetic resonance studies at 90.5 MHz of the basic pancreatic trypsin inhibitor.
107.: Nagayama, K., Bachmann, P., Wüthrich, K. and Ernst, R.R. (1978) J. Magn. Reson. 31,
133-148.
The use of cross sections and of projections in two-dimensional NMR spectroscopy.
108.: Keller, R.M. and Wüthrich, K. (1978) Biochem. Biophys. Res. Comm. 83, 1132-1139.
Evolutionary change of the heme c electronic structure: ferricytochrome c-551 from Pseudomonas aeruginosa and horse heart ferricytochrome c.
109.: Wagner, G., Wüthrich, K. and Tschesche, H. (1978) Eur. J. Biochem. 89, 367-377.
A 1H nuclear magnetic resonance study of the solution conformation of the isoinhibitor K from Helix pomatia.
110.: Wagner, G. and Wüthrich, K. (1978) Nature 275, 247-248.
Dynamic model of globular protein conformations based on NMR studies in solution.
111.: Lauterwein, J. and Wüthrich, K. (1978) FEBS Lett. 93, 181-184.
A possible structural basis for the different modes of action of neurotoxins and cardiotoxins from snake venoms.
112.: Wüthrich, K. and Wagner, G. (1978) Trends Biochem. Sci. 3, 227-230.
Internal motion in globular proteins.
113.: Richarz, R. and Wüthrich, K. (1978) Biopolymers 17, 2133-2141.
Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH.
114.: Wüthrich, K., Wagner, G. and Bundi, A. (1978) in Nuclear Magnetic Resonance Spectroscopy in Molecular Biology (B. Pullman, ed.) pp. 201-210, Reidel, Dordrecht.
NMR studies of the molecular dynamics of peptides and proteins.
115.: Bundi, A., Andreatta, R.H. and Wüthrich, K. (1978) Eur. J. Biochem. 91, 201-208.
Characterisation of a local structure in the synthetic parathyroid hormone fragment 1-34 by 1H nuclear magnetic resonance techniques.
116.: Bösch, C., Bundi, A., Oppliger, M. and Wüthrich, K. (1978) Eur. J. Biochem. 91, 209-214.
1H nuclear magnetic resonance studies of the molecular conformation of monomeric glucagon in aqueous solution.
117.: Perkins, S.J. and Wüthrich, K. (1978) Biochim. Biophys. Acta 536, 406-420.
Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by 1H NMR at 360 MHz.
118.: Gordon, S.L. and Wüthrich, K. (1978) J. Am. Chem. Soc. 100, 7094-7096.
Transient proton-proton Overhauser effects in horse ferrocytochrome c.
119.: DeMarco, A., Llinás, M. and Wüthrich, K. (1978) Biopolymers 17, 2727-2742.
1H-15N spin-spin couplings in alumichrome.
120.: Lauterwein, J., Lazdunski, M. and Wüthrich, K. (1978) Eur. J. Biochem. 92, 361-71.
The 1H nuclear magnetic resonance spectra of neurotoxin I and cardiotoxin VII4 from Naja mossambica mossambica.
121.: Llinás, M., Klein, M.P. and Wüthrich, K. (1978) Biophys. J. 24, 849-862.
Amide proton spin-lattice relaxation in polypeptides: a field-dependence study of the proton and nitrogen dipolar interactions in alumichrome.
122.: Viti, V., Wüthrich, K., Giacometti, G. and Brunori, M. (1978) in Proceedings of the European Conference on NMR of Macromolecules (F. Conti, ed.) pp. 509-516, Lerici, Sassari, Italy.
1H NMR studies of structural aspects of the root effect in trout hemoglobin.
123.: Nagayama, K., Bachmann, P., Ernst, R.R. and Wüthrich, K. (1979) Biochem. Biophys. Res. Comm. 86, 218-225.
Selective spin decoupling in the J-resolved two-dimensional 1H NMR spectra of proteins.
124.: Perkins, S.J. and Wüthrich, K. (1979) Biochim. Biophys. Acta 576, 409-423.
Ring current effects in the conformation-dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor.
125.: Bundi, A. and Wüthrich, K. (1979) Biopolymers 18, 285-297.
1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH.
126.: Bundi, A. and Wüthrich, K. (1979) Biopolymers 18, 299-311.
Use of amide 1H NMR titration shifts for studies of polypeptide conformation.
127.: Wüthrich, K., Wagner, G. and Richarz, R. (1979) in Protein: Structure, Function and Industrial Applications (E. Hofmann, W. Pfeil and H. Aurich, eds.) pp. 143-152, Pergamon, New York.
A dynamic model for globular protein conformations based on high resolution NMR data.
128.: Wüthrich, K., Keller, R.M. and Gordon, S.L. (1978) in Frontiers of Biological Energetics, (P.L. Dutton, J. Leigh and A. Scarpa, eds.) Vol. I, pp. 109-117, Academic Press, New York.
Evolutionary changes of the heme c electronic structure in cytochromes c.
129.: Dubs, A., Wagner, G. and Wüthrich, K. (1979) Biochim. Biophys. Acta 577, 177-194.
Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor.
130.: Wagner, G., Tschesche, H. and Wüthrich, K. (1979) Eur. J. Biochem. 95, 239-248.
The influence of localized chemical modifications of the basic pancreatic trypsin inhibitor on static and dynamic aspects of the molecular conformation in solution.
131.: Wagner, G., Kalb (Gilboa), A.J. and Wüthrich, K. (1979) Eur. J. Biochem. 95, 249-253.
Conformational studies by 1H nuclear magnetic resonance of the basic pancreatic trypsin inhibitor after reduction of the disulfide bond between Cys-14 and Cys-38.
132.: Wagner , G. and Wüthrich, K. (1979) J. Magn. Reson. 33, 675-680.
Truncated driven nuclear Overhauser effect (TOE): a new technique for studies of selective 1H-1H Overhauser effects in the presence of spin diffusion.
133.: Wüthrich, K. and Wagner, G. (1979) J. Mol. Biol. 130, 1-18.
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
134.: Richarz, R., Sehr, P., Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 130, 19-30.
Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor.
135.: Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 130, 31-37.
Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.
136.: Wüthrich, K., Nagayama, K. and Ernst, R.R. (1979) Trends Biochem. Sci. 4, N178-N181.
Two-dimensional NMR spectroscopy.
137.: Nagayama, K., Wüthrich, K. and Ernst, R.R. (1979) Biochem. Biophys. Res. Comm. 90, 305-311.
Two-dimensional spin echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromolecules.
138.: Lauterwein, J., Bösch, C., Brown, L.R. and Wüthrich, K. (1979) Biochim. Biophys. Acta 556, 244-264.
Physicochemical studies of the protein-lipid interactions in melittin-containing micelles.
139.: Keller, R.M., Picot, D. and Wüthrich, K. (1979) Biochim. Biophys. Acta 580, 259-265.
Individual assignments of the heme resonances in the 360 MHz 1H NMR spectra of cytochrome c-557 from Crithidia oncopelti.
140.: Hetzel, R. and Wüthrich, K. (1979) Biopolymers 18, 2589-2606.
Conformational energy studies of linear dipeptides H-X-L-Pro-OH.
141.: Wagner, G. and Wüthrich, K. (1979) J. Mol. Biol. 134, 75-94.
Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins.
142.: Ernst, R.R., Aue, W.P., Bachmann, P., Höhener, A., Linder, M., Meier, B., Müller, L., Wokaun, A., Nagayama, K., Wüthrich, K. and Jeener, J. (1978) Proc. XXth Congress AMPERE, Tallinn, 15-18.
Applications of two-dimensional spectroscopy to problems of physical, chemical and biological relevance.
143.: Vas/ ák, M., Nagayama, K., Wüthrich, K., Mertens, M.L. and Kägi, J.H.R. (1979) Biochemistry 18, 5050-5055.
Creatine kinase: nuclear magnetic resonance and fluorescence evidence for interactions of adenosine 5'-diphosphate with aromatic residues.
144.: Richarz, R., Tschesche, H. and Wüthrich, K. (1979) Eur. J. Biochem. 102, 563-571.
Structural characterization by nuclear magnetic resonance of a reactive-site carbon-13-labelled basic pancreatic trypsin inhibitor with the peptide bond Arg-39 - Ala-40 cleaved and Arg-39 removed.
145.: Wüthrich, K. (1979) 355 pages, Tokyo, Japan
146.: Keller, R.M. and Wüthrich, K. (1980) Biochim. Biophys. Acta 621, 204-217.
Structural study of the heme crevice in cytochrome b5 based on individual assignments of the 1H NMR lines of the heme group and selected amino acid residues.
147.: Wüthrich, K., Roder, H. and Wagner, G. (1980) in Protein Folding (R. Jaenicke, ed.) pp. 549-564, North-Holland, Amsterdam.
Internal mobility and unfolding of globular proteins.
148.: Senn, H., Keller, R.M. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 92,
1362-1369.
Different chirality of the axial methionine in homologous cytochromes c determined by
1H NMR and CD spectroscopy.
149.: Wüthrich, K. (1980) in Frontiers of Bioorganic Chemistry and Molecular Biology (S.N. Ananchenko, ed.) pp. 161-168, Pergamon Press, Oxford.
Complementation of protein crystal structures by NMR studies in solution.
150.: Lauterwein, J., Brown, L.R. and Wüthrich, K. (1980) Biochim. Biophys. Acta 622, 219-230.
High-resolution 1H NMR studies of monomeric melittin in aqueous solution.
151.: Brown, L.R., Lauterwein, J. and Wüthrich, K. (1980) Biochim. Biophys. Acta 622, 231-244.
High-resolution 1H NMR studies of self-aggregation of melittin in aqueous solution.
152.: Perkins, S.J. and Wüthrich, K. (1980) J. Mol. Biol. 138, 43-64.
Conformational transition from trypsinogen to trypsin: 1H nuclear magnetic resonance at 360 MHz and ring current calculations.
153.: Anil-Kumar, Ernst, R.R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 95, 1-6.
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules.
154.: Wüthrich, K., Bösch, C. and Brown, L.R. (1980) Biochem. Biophys. Res. Comm. 95,
1504-1509.
Conformational studies of lipid-bound polypeptides by elucidation of proton-proton cross-relaxation networks.
155.: Nagayama, K., Anil-Kumar, Wüthrich, K. and Ernst, R.R. (1980) J. Magn. Reson. 40, 321-334.
Experimental techniques of two-dimensional correlated spectroscopy.
156.: Anil-Kumar, Wagner, G., Ernst, R.R. and Wüthrich, K. (1980) Biochem. Biophys. Res. Comm. 96, 1156-1163.
Studies of J-connectivities and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments.
157.: Wüthrich, K., Wagner, G., Richarz, R. and Braun, W. (1980) Biophys. J. 32, 549-560.
Correlations between internal mobility and stability of globular proteins.
158.: Keller, R.M., Schejter, A. and Wüthrich, K. (1980) Biochim. Biophys. Acta 626, 15-22.
1H NMR studies of the coordination geometry at the heme iron and the electronic structure of the heme group in cytochrome c-552 from Euglena gracilis.
159.: Grathwohl, C. and Wüthrich, K. (1981) in Perspectives in Peptide Chemistry (A. Eberle,
R. Geiger and T. Wieland, eds.) pp. 249-260, Karger, Basel.
Nuclear magnetic resonance studies of peptide and protein conformations.
160.: Richarz, R., Nagayama, K. and Wüthrich, K. (1980) Biochemistry 19, 5189-5196.
Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analogue.
161.: Richarz, R., Tschesche, H. and Wüthrich, K. (1980) Biochemistry 19, 5711-5715.
Carbon-13 nuclear magnetic resonance studies of the selectively isotope-labeled reactive site peptide bond of the basic pancreatic trypsin inhibitor in the complexes with trypsin, trypsinogen and anhydrotrypsin.
162.: Wüthrich, K., Eugster, A. and Wagner, G. (1980) J. Mol. Biol. 144, 601-604.
p2H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 14-38.
163.: Bösch, C., Brown, L.R. and Wüthrich, K. (1980) Biochim. Biophys. Acta 603, 298-312.
Physicochemical characterization of glucagon-containing lipid micelles.
164.: Wüthrich, K. and Wagner, G. (1980) in Biomolecular Structure, Conformation, Function and Evolution, Vol. 2: Physico-Chemical and Theoretical Studies (R. Srinivasan, ed.)
pp. 23-29, Pergamon Press, Oxford.
Dynamic aspects of protein conformation studied by nuclear magnetic resonance techniques: evidence for hydrophobic stability domains in globular proteins.
165.: Nagayama, K. and Wüthrich, K. (1981) Eur. J. Biochem. 114, 365-374.
Systematic application of two-dimensional 1H nuclear magnetic resonance techniques for studies of proteins 1: combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino acid residues.
166.: Wagner, G., Anil-Kumar and Wüthrich, K. (1981) Eur. J. Biochem. 114, 375-384.
Systematic application of two-dimensional 1H nuclear magnetic resonance techniques for studies of proteins 2: combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidation of polypeptide secondary structures.
167.: Braun, W., Bösch, C., Brown, L.R., Go , N. and Wüthrich, K. (1981) Biochim. Biophys. Acta 667, 377-396.
Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations: application to micelle-bound glucagon.
168.: Bösch, C., Anil-Kumar, Baumann, R., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 42, 159-163.
Comparison of selective proton-proton Overhauser effects in biological macromolecules observed by one-dimensional and two-dimensional NMR experiments.
169.: Wider, G., Baumann, R., Nagayama, K., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 42, 73-87.
Strong spin-spin coupling in the two-dimensional J-resolved 360 MHz 1H NMR spectra of the common amino acids.
170.: Brown, L.R., Bösch, C. and Wüthrich, K. (1981) Biochim. Biophys. Acta 642, 296-312.
Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine: EPR and NMR studies.
171.: Nagayama, K. and Wüthrich, K. (1981) Eur. J. Biochem. 115, 653-657 .
Structural interpretation of vincinal proton-proton coupling constants 3Jab in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy.
172.: Keller, R.M. and Wüthrich, K. (1981) Biochim. Biophys. Acta 668, 307-320.
1H NMR studies of structural homologies between the heme environments in horse cytochrome c and in cytochrome c-552 from Euglena gracilis.
173.: Wüthrich, K. (1981) in Lectures Delivered at the International Winter School on Current Trends in Biomolecular Structures (R. Srinivasan, ed.) pp. 271-293, Macmillan India, Madras.
High resolution nuclear magnetic resonance (NMR) studies of peptides and proteins.
174.: Anil-Kumar, Wagner, G., Ernst, R.R. and Wüthrich, K. (1981) J. Am. Chem. Soc. 103, 3654-3658.
Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation.
175.: Possani, L., Steinmetz, W.E., Dent, M.A.R., Alagón, A.C. and Wüthrich, K. (1981) Biochim. Biophys. Acta 669, 183-192.
Preliminary spectroscopic characterization of six toxins from latin american scorpions.
176.: Baumann, R., Anil-Kumar, Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 44, 76-83.
Improvement of 2D NOE and 2D correlated spectra by triangular multiplication.
177.: Keller, R.M. and Wüthrich, K. (1981) in Biological Magnetic Resonance (L.J. Berliner and J. Reuben, eds.) Vol. 3, 1-52, Plenum Press, New York.
Multiple irradiation 1H NMR experiments with hemoproteins.
178.: Nagayama, K. and Wüthrich, K. (1980) in Protein Dynamics and Energy Transduction, pp. 83-12, Taniguchi Foundation, Osaka.
An application of two-dimensional NMR techniques for studies of the rotational mobility of the amino acid side chains about the Ca-Cb bonds in basic pancreatic trypsin inhibitor.
179.: Wüthrich, K., Richarz, R., Perkins, S.J. and Tschesche, H. (1981) in Structural Aspects of Recognition and Assembly in Biological Macromolecules (M. Balaban, J.L. Sussman, W. Traub and A. Yonath, eds.) pp. 21-34, Balaban ISS, Rehovot.
Protein-protein interactions in the complexes formed between the basic pancreatic trypsin inhibitor (BPTI) and trypsin or trypsinogen: studies in solution by 13C NMR and 1H NMR.
180.: Baumann, R., Wider, G., Ernst, R.R. and Wüthrich, K. (1981) J. Magn. Reson. 44, 402-406.
Improvement of 2D NOE and 2D correlated spectra by symmetrization.
181.: Brown, L.R. and Wüthrich, K. (1981) Biochim. Biophys. Acta 647, 95-111.
Melittin bound to dodecylphosphocholine micelles: 1H NMR assignments and global conformational features.
182.: Wüthrich, K. (1981) Biochem. Soc. Symp. 46, 17-37.
Nuclear magnetic resonance studies of internal mobility in globular proteins.
183.: Grathwohl, C. and Wüthrich, K. (1981) Biopolymers 20, 2623-2633.
NMR studies of the rates of proline cis-trans isomerization in oligopeptides.
184.: Steinmetz, W.E., Moonen, X., Anil-Kumar, Lazdunski, M., Visser, L., Carlsson, F.H.H. and Wüthrich, K. (1981) Eur. J. Biochem. 120, 467-475.
1H nuclear magnetic resonance studies of the conformation of cardiotoxin VII2 from Naja mossambica mossambica.
185.: Brown, L.R., Braun, W., Anil-Kumar and Wüthrich, K. (1982) Biophys. J. 37, 319-328.
High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.
186.: Macura, S., Wüthrich, K. and Ernst, R.R. (1982) J. Magn. Reson. 46, 269-282.
Separation and suppression of coherent transfer effects in two-dimensional NOE and chemical exchange spectroscopy.
187.: Wüthrich, K., Wider, G., Wagner, G. and Braun, W. (1982) J. Mol. Biol. 155, 311-319.
Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance.
188.: Billeter, M., Braun, W. and Wüthrich, K. (1982) J. Mol. Biol. 155, 321-346.
Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra: computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.
189.: Wagner, G. and Wüthrich, K. (1982) J. Mol. Biol. 155, 347-366.
Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra: basic pancreatic trypsin inhibitor.
190.: Wider, G., Lee, K.H. and Wüthrich, K. (1982) J. Mol. Biol. 155, 367-388.
Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra: glucagon bound to perdeuterated dodecylphosphocholine micelles.
191.: Macura, S., Wüthrich, K. and Ernst, R.R. (1982) J. Magn. Reson. 47, 351-357.
The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules.
192.: Wüthrich, K. (1982) in Structural Molecular Biology (D.B. Davies, W. Saenger and S.S. Danyluk, eds.) pp. 215-235 Plenum Press, New York.
High resolution NMR experiments for studies of protein conformations.
193.: Arseniev, A.S., Wider, G., Joubert, F.J. and Wüthrich, K. (1982) J. Mol. Biol. 159, 323-351.
Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis: two-dimensional nuclear magnetic resonance at 500 MHz.
194.: Wagner, G. and Wüthrich, K. (1982) J. Mol. Biol. 160, 343-361.
Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution: studies with two-dimensional nuclear magnetic resonance.
195.: Wüthrich, K. (1982) Die Umschau 82, 684-690.
Die Struktur von nicht-kristallinen Proteinen.
196.: Keller, R.M., Baumann, R., Hunziker-Kwik, E.H., Joubert , F.J. and Wüthrich, K. (1983) J. Mol. Biol. 163, 623-646.
Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor homologue K from Dendroaspis polylepis polylepis: two-dimensional nuclear magnetic resonance at 360 and 500 MHz.
197.: Wüthrich, K., Bösch, C., Braun, W., Brown, L.R., Lee, K.H. and Wider, G. (1982) in Structure of Complexes between Biopolymers and Low Molecular Weight Molecules, (W. Bartmann and G. Snatzke, eds.) pp. 45-155, Wiley, New York.
NMR studies of the conformation of polypeptide chains bound to lipid micelles.
198.: Wüthrich, K. and Wagner, G. (1983) in Mobility and Function in Proteins and Nucleic Acids (R. Porter, M. O'Connor and J. Whelan, eds.) pp. 310-328, Pitman, London.
Nuclear magnetic resonance studies of mobility in proteins.
199.: Hosur, R.V., Wider, G. and Wüthrich, K. (1983) Eur. J. Biochem. 130, 497-508 .
Sequential individual resonance assignments in the 1H nuclear magnetic resonance spectrum of cardiotoxin VII2 from Naja mossambica mossambica.
200.: Senn, H., Eugster, A. and Wüthrich, K. (1983) Biochim. Biophys. Acta 743, 58-68.
Determination of the coordination geometry at the heme iron in three cytochromes c from Saccharomyces cerevisiae and from Cadida krusei based on individual 1H NMR assignments for heme c and the axially coordinated amino acids.
201.: Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 743, 69-81.
Individual 1H 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 two isocytochromes c-551 from Rhodopseudomonas gelatinosa.
202.: Wagner, G. und Wüthrich, K. (1983) Naturwissenschaften 70, 105-114 .
Dynamik von Protein-Strukturen.
203.: Wüthrich, K. (1983) Biopolymers 22, 131-138.
Sequential individual resonance assignments in the 1H-NMR spectra of polypeptides and proteins.
204.: Wider, G., Hosur, R.V. and Wüthrich, K. (1983) J. Magn. Reson. 52, 13-135.
Suppression of the solvent resonance in 2D NMR spectra of proteins in H2O solution.
205.: Wüthrich, K. (1983) in Fortschrittsberichte aus Naturwissenschaft und Medizin (H.A. Staab, W. Gerok, H. Markl, W. Martienssen und H. Gibian, eds.) pp. 169-182, Wissenschaftliche Verlagsgesellschaft, Stuttgart.
Räumliche Struktur von Proteinen in Lösung und in Lipid-Wasser-Grenzschichten.
206.: Pardi, A., Walker, R., Rapoport, H., Wider, G. and Wüthrich, K. (1983) J. Am. Chem. Soc. 105, 1652-1653.
Sequential assignments for the 1H and 31P atoms in the backbone of oligonucleotides by two-dimensional nuclear magnetic resonance.
207.: Strop , P. and Wüthrich, K. (1983) J. Mol. Biol. 166, 631-640.
Characterization of the proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance: stability, amide proton exchange and mobility of aromatic residues.
208.: Strop , P., Wider, G. and Wüthrich, K. (1983) J. Mol. Biol. 166, 641-667.
Assignment of the 1H nuclear magnetic resonance spectrum of the proteinase inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic resonance at 500 MHz.
209.: Strop , P., /Cechová , D. and Wüthrich, K. (1983) J. Mol. Biol. 166, 669-676.
Preliminary structural comparison of the proteinase isoinhibitors IIA and IIB from bull seminal plasma based on individual assignments of the 1H nuclear magnetic resonance spectra by two-dimensional nuclear magnetic resonance at 500 MHz.
210.: Marion, D. and Wüthrich, K. (1983) Biochem. Biophys. Res. Comm. 113, 967-974.
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.
211.: Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 746, 48-60.
Conformation of the axially bound ligands of the heme iron and electronic structure of
heme c in the cytochromes c-551 from Pseudomonas mendocina and Pseudomonas stutzeri and in cytochrome c from Rhodospirillum rubrum.
212.: Senn, H. and Wüthrich, K. (1983) Biochim. Biophys. Acta 747, 16-25.
A new spatial structure for the axial methionine observed in cytochrome c5 from Pseudomonas mendocina: correlations with the electronic structure of heme c.
213.: Hosur, R.V., Ernst, R.R. and Wüthrich, K. (1983) J. Magn. Reson. 54, 142-145.
A simple two-dimensional measurement of the decoupler power during continuous homonuclear irradiation for the correction of Bloch-Siegert shifts.
214.: Wagner, G., Pardi, A. and Wüthrich, K. (1983) J. Am. Chem. Soc. 105, 5948-5949.
Hydrogen bond length and 1H NMR chemical shifts in proteins.
215.: Braun, W., Wider, G., Lee, K.H. and Wüthrich, K. (1983[) J. Mol. Biol. 169, 921-948.
Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
216.: Wüthrich, K., Billeter, M. and Braun, W. (1983) J. Mol. Biol. 169, 949-961.
Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.
217.: Zuiderweg, E.R.P., Kaptein, R. and Wüthrich, K. (1983) Proc. Natl. Acad. Sci. USA 80, 5837-5841.
Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution.
218.: Senn, H., Guerlesquin, F., Bruschi, M. and Wüthrich, K. (1983) Biochim. Biophys. Acta 748, 194-204.
Coordination of the heme iron in the low-potential cytochrome c-553 from Desulfovibrio vulgaris and Desulfovibrio desulfuricans. Different chirality of the axially bound methionine in the oxidized and reduced states.
219.: Zuiderweg, E.R.P., Kaptein, R. and Wüthrich, K. (1983) Eur. J. Biochem. 137, 279-292.
Sequence-specific resonance assignments in the 1H nuclear magnetic resonance spectrum of the lac repressor DNA-Binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy.
220.: Pardi, A., Wagner, G. and Wüthrich, K. (1983) Eur. J. Biochem. 137, 445-454.
Protein conformation and proton nuclear magnetic resonance chemical shifts.
221.: Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R. and Wüthrich, K. (1983) Biochem. Biophys. Res. Comm. 117, 479-485.
Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering.
222.: Wider, G., Macura, S., Anil Kumar, Ernst, R.R. and Wüthrich, K. (1984) J. Magn. Reson. 56, 207-234.
Homonuclear two-dimensional 1H NMR of proteins: experimental procedures.
223.: Senn, H., Cusanovich, M.A. and Wüthrich, K. (1984) Biochim. Biophys. Acta 785, 46-53.
1H NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555.
224.: Williamson, M.P., Marion, D. and Wüthrich, K. (1984) J. Mol. Biol. 173, 341-359.
Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance.
225.: Neuhaus, D., Wider, G., Wagner, G. and Wüthrich, K. (1984) J. Magn. Reson. 57, 164-168.
X-relayed 1H-1H correlated spectroscopy.
226.: Wüthrich, K. and Wagner, G. (1984) Trends Biochem. Sci. 9, 152-154.
Internal dynamics of proteins.
227.: Senn, H., Billeter, M. and Wüthrich, K. (1984) Eur. Biophys. J. 11, 3-15.
The spatial structure of the axially bound methionine in solution conformations of horse ferrocytochrome c and Pseudomonas aeruginosa ferrocytochrome c 551 by 1H NMR.
228.: Wüthrich, K., Strop,, P., Ebina, S. and Williamson, M.P. (1984) Biochem. Biophys. Res. Comm. 122, 1174-1178.
A globular protein with slower amide proton exchange from an a helix than from antiparallel b sheets.
229.: Rance, M., Wagner, G., Sørensen, O.W., Wüthrich, K. and Ernst, R.R. (1984) J. Magn. Reson. 59, 250-261.
Applications of w1-decoupled 2D correlation spectra to the study of proteins.
230.: Senn, H., Böhme, H. and Wüthrich, K. (1984) Biochim. Biophys. Acta 789, 311-323.
Studies of the solution conformation of Spirulina platensis cytochrome c-553 by 1H nuclear magnetic resonance and circular dichroism.
231.: Neuhaus, D., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1984) Eur. J. Biochem. 143, 659-667.
113Cd-1H spin-spin couplings in homonuclear 1H correlated spectroscopy of metallothionein: identification of the cysteine 1H spin systems.
232.: Zuiderweg, E.R.P., Billeter, M., Boelens, R., Scheek, R.M., Wüthrich, K. and Kaptein, R. (1984) FEBS Lett. 174, 243-247.
Spatial arrangement of the three a helices in the solution conformation of E. coli lac repressor DNA-binding domain.
233.: Havel, T.F. and Wüthrich, K. (1984) Bull. Math. Biol. 46, 673-698.
A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular 1H-1H proximities in solution.
234.: Stassinopoulou, C.I., Wagner, G. and Wüthrich, K. (1984) Eur. J. Biochem. 145, 423-430.
Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor: sequence specific resonance assignments and sequence location of conformation changes relative to the native protein.
235.: Wagner, G., Stassinopoulou, C.I. and Wüthrich, K. (1984) Eur. J. Biochem. 145, 431-436.
Amide proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor.
236.: Ebina, E. and Wüthrich, K. (1984) J. Mol. Biol. 179, 283-288.
Amide proton titration shifts in bull seminal inhibitor IIA by two-dimensional correlated 1H nuclear magnetic resonance (COSY): manifestation of conformational equilibria involving carboxylate groups.
237.: Bodenhausen, G., Wagner, G., Rance, M., Sørensen, O.W., Wüthrich , K. and Ernst, R.R. (1984) J. Magn. Reson. 59, 542-550.
Longitudinal two-spin order in 2D exchange spectroscopy (NOESY).
238.: Zuiderweg, E.R.P., Billeter, M. Kaptein, R., Boelens, R., Scheek , R.M. and Wüthrich, K. (1984) in Progress in Bioorganic Chemistry and Molecular Biology (Yu.A. Ovchinnikov, ed.) pp. 65- 70, Elsevier, Amsterdam.
Solution conformation of E. coli lac repressor DNA-binding domain by 2D NMR: sequence location and spatial arrangement of three a-helices.
239.: Wüthrich, K. (1981) Makromol. Chem. Suppl. 5, 234-252.
Studies of static and dynamic aspects of spatial protein structures by high resolution nuclear magnetic resonance spectroscopy.
240.: Wüthrich, K., Billeter, M. and Braun, W. (1984) J. Mol. Biol. 180, 715-740.
Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances.
241.: Pardi, A., Billeter, M. and Wüthrich, K. (1984) J. Mol. Biol. 180, 741-751.
Calibration of the angular dependence of the amide proton-Ca proton coupling constants, 3JHNa , in a globular protein: use of 3JHNa for identification of helical secondary structure.
242.: Rance, M., Sørensen, O.W., Leupin, W., Kogler, H., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 61, 67-80.
Uniform exitation of multiple quantum coherence: application to two-dimensional double- quantum spectroscopy.
243.: Wüthrich, K. (1984) Biomed. Res. 5, 151-160.
Three-dimensional structure of non crystalline polypeptides by nuclear magnetic resonance.
244.: Havel , T.F. and Wüthrich, K. (1985) J. Mol. Biol. 182, 281-294.
An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution.
245.: Williamson, M.P., Havel, T.F. and Wüthrich, K. (1985) J. Mol. Biol. 182, 295-315.
Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.
246.: Kline, A.D. and Wüthrich, K. (1985) J. Mol. Biol. 183, 503-507.
Secondary structure of the a-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance.
247.: Denk, W., Wagner, G., Rance, M. and Wüthrich, K. (1985) J. Magn. Reson. 62, 350-355.
Combined suppression of diagonal peaks and t1-ridges in two-dimensional nuclear Overhauser enhancement spectra.
248.: Billeter, M., Engeli, M. and Wüthrich, K. (1985) J. Mol. Graphics 3, 79-83, 97-98.
Interactive program for investigation of protein structures based on 1H NMR experiments.
249.: Roder, H., Wagner, G. and Wüthrich, K. (1985) Biochemistry 24, 7396-7407.
Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.
250.: Roder, H., Wagner, G. and Wüthrich, K. (1985) Biochemistry 24, 7407-7411.
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor.
251.: Rance, M., Bodenhausen, G., Wagner, G., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 62, 497-510.
A systematic approach to the suppression of J cross peaks in 2D exchange and 2D NOE spectroscopy.
252.: Guerlesquin, F., Bruschi, M. and Wüthrich, K. (1985) Biochim. Biophys. Acta 830,
296-303.
1H NMR studies of Desulfovibrio desulfuricans Norway strain cytochrome c3.
253.: Müller, N., Bodenhausen, G., Wüthrich, K. and Ernst, R.R. (1985) J. Magn. Reson. 65,
531-534.
The appearance of forbidden cross peaks in two-dimensional nuclear magnetic resonance spectra due to multiexponential T2 relaxation.
254.: Frey, M.H., Leupin, W., Sørensen, O.W., Denny, W.A., Ernst, R.R. and Wüthrich, K. (1985) Biopolymers 24, 2371-2380.
Sequence-specific assignment of the backbone 1H- and 31P-NMR lines in a short DNA duplex with homo- and heteronuclear correlated spectroscopy.
255.: Chazin, W.J., Goldenberg, D.P., Creighton, T.E. and Wüthrich, K. (1985) Eur. J. Biochem. 152, 429-437.
Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution.
256.: Wagner, G. , Bodenhausen, G., Müller, N., Rance, M., Sørensen, O.W., Ernst, R.R. and Wüthrich, K. (1985) J. Am. Chem. Soc. 107, 6440-6446.
Exchange of two-spin order in nuclear magnetic resonance: separation of exchange and cross relaxation processes.
257.: Frey, M.H., Wagner, G., Vas/ ák, M., Sørensen, O.W., Neuhaus, D., Wörgötter, E., Kägi, J.H.R., Ernst, R.R. and Wüthrich, K. (1985) J. Amer. Chem. Soc. 107, 6847-6851.
Polypeptide metal cluster connectivities in metallothionein-2 by novel 1H-113Cd heteronuclear two-dimensional NMR experiments.
258.: Neuhaus, D., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1985) Eur. J. Biochem. 151, 257-273.
Systematic application of high resolution, phase-sensitive two- dimensional 1H NMR techniques for the identification of the amino acid proton spin systems in proteins: rabbit metallothionein-2.
259.: Wüthrich, K. (1986) Europhysics News 17, 11-13.
NMR with proteins and nucleic acids.
260.: Braun, W., Wagner, G., Wörgötter, E., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1986) J. Mol. Biol. 187, 125-129.
Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution.
261.: Wagner, G., Neuhaus, D., Wörgötter, E., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K.
(1986) J. Mol. Biol. 187, 131-135.
Nuclear magnetic resonance identification of ``half-turn'' and 310 -helix secondary structure in rabbit liver metallothionein-2.
262.: Senn, H. and Wüthrich, K. (1985) Q. Rev. Biophys. 18, 111-134.
Amino acid sequence, haem iron coordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes.
263.: Otting, G., Widmer, H., Wagner, G. and Wüthrich, K. (1986) J. Magn. Reson. 66, 187-193.
Origin of t1 and t2 ridges in 2D NMR spectra and procedures for suppression.
264.: Otting, G. and Wüthrich, K. (1986) J. Magn. Reson. 66, 359-363.
Complete protein fingerprints by double quantum spectroscopy.
265.: Wagner, G., Neuhaus, D., Wörgötter, E., Vas/ ák, M., Kägi , J.H.R. and Wüthrich, K. (1986) Eur. J. Biochem. 157, 275-289.
Sequence-specific 1H NMR assignments in rabbit liver metallothionein-2.
266.: Schultze, P. and Wüthrich, K. (1986) J. Mol. Graphics 4, 105-111.
Display algorithm for space filling molecular models using a video array processor.
267.: Kline, A.D., Braun, W. and Wüthrich, K. (1986) J. Mol. Biol. 189, 377-382.
Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the a-amylase inhibitor Tendamistat.
268.: Wagner, G. and Wüthrich, K. (1986) Eur. J. Biochem. 157, 618.
Reply to the comments by C.E. Dempsey on ``Amide proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor'', by G. Wagner, C.I. Stassinopoulou and K. Wüthrich.
269.: Wüthrich, K. (1986) in NMR in the Life Sciences (E.M. Bradbury and C. Nicolini, eds.)
NATO ASI Series A: Life Sciences 107, 11-22, Plenum Press, New York.
2D NMR with biopolymers.
270.: Wüthrich, K. (1986) in Design and Synthesis of Organic Molecules Based on Molecular Recognition, Proc. XVIIth Solvay Conference on Chemistry (G. van Binst, ed.) pp. 52-56, Springer, Berlin.
Glucagon conformation in different environments: implications for molecular recognition.
271.: Chazin, W.J., Wüthrich, K., Hyberts, S., Rance, M., Denny, W.A. and Leupin, W. (1986) J. Mol. Biol. 190, 439-453.
1H nuclear magnetic resonance assignments for d-(GCATTAATGC)2 using experimental refinements of established procedures.
272.: Roder, H. and Wüthrich, K. (1986) Proteins 1, 34-42.
Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons.
273.: Wüthrich, K. (1986) NMR of proteins and nucleic acids, 292 pages , Wiley, New York.
274.: Wüthrich, K. (1986) in X National NMR Symposium of Finland (E. Kolehmainen, ed.)
pp. 1-23, Publications of the University of Kuopio, Vol. 3, Kuopio.
Nuclear magnetic resonance with proteins and nucleic acids.
275.: Wörgötter, E., Wagner, G. and Wüthrich, K. (1986) J. Am. Chem. Soc. 108, 6162- 6167.
Simplification of two-dimensional 1H NMR spectra using an X-filter.
276.: Müller, N., Ernst, R.R. and Wüthrich, K. (1986) J. Am. Chem. Soc. 108, 6482-6492.
Multiple-quantum-filtered two-dimensional correlated NMR spectroscopy of proteins.
277.: Leupin, W., Chazin, W.J., Hyberts, S., Denny, W.A. and Wüthrich, K. (1986) Biochemistry 25, 5902-5910.
NMR studies of the complex between the decadeoxynucleotide d-(GCATTAATGC)2 and a minor-groove-binding drug.
278.: Wagner, G. and Wüthrich, K. (1986) in Enzyme Structure, Part L (C.H.W. Hirs and S.N. Timasheff, eds.) Methods in Enzymology 131, 307-326.
Observation of internal motility of proteins by nuclear magnetic resonance in solution.
279.: Montelione, G.T., Wüthrich, K., Nice, E.C., Burgess, A.W. and Scheraga, H.A. (1986) Proc. Natl. Acad. Sci. USA 83, 8594-8598.
Identification of two antiparallel b-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.
280.: Widmer, H. and Wüthrich, K. (1986) J. Magn. Reson. 70, 270-279.
Simulation of two-dimensional NMR experiments using numerical density matrix calculations.
281.: Kline, A.D. and Wüthrich, K. (1986) J. Mol. Biol. 192, 869-890.
Complete sequence-specific 1H nuclear magnetic resonance assignments for the
a-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae.
282.: Senn, H., Eugster, A., Otting, G., Suter, F. and Wüthrich, K. (1987) Eur. Biophys. J. 14,
301-306.
15N-labeled P22 c2 repressor for nuclear magnetic resonance studies of protein-DNA interactions.
283.: Otting, G., Senn, H., Wagner, G. and Wüthrich, K. (1986) J.Magn. Reson. 70, 500-505.
Editing of 2D 1H NMR spectra using X half-filters: combined use with residue-selective 15N-labeling of proteins.
284.: Senn, H., Otting, G. and Wüthrich, K. (1987) J. Am. Chem. Soc. 109, 1090-1092.
Protein structure and interactions by combined used of sequential NMR assignments and isotope labeling.
285.: Leupin, W., Wagner, G., Denny , W.A. and Wüthrich, K. (1987) Nucl. Acids Res. 15,
267-275.
Assignment of the 13C nuclear magnetic resonance spectrum of a short DNA-duplex with 1H detected two-dimensional heteronuclear correlation spectroscopy.
286.: Wüthrich, K. (1987) in Structure, Dynamics and Function of Biomolecules (A. Ehrenberg, R. Rigler, A. Gräslund and L. Nilsson, eds.) pp. 104-107, Springer, Berlin.
A NMR view of proteins in solution.
287.: Wüthrich, K. (1986) Rev. Magn. Reson. in Medicine 1, 1-20 .
Structure and function of proteins and nucleic acids viewed by NMR in solution.
288.: Wüthrich, K. (1986) in Structure and Dynamics of Nucleic Acids, Proteins and Membranes, (E. Clementi and S. Chin, eds.) pp. 21-29, Plenum Press, New York.
Conformation of non-crystalline proteins viewed by NMR.
289.: Billeter, M., Havel, T.F. and Wüthrich, K. (1987) J. Comp. Chem. 8, 132-141.
The ellipsoid algorithm as a method for the determination of polypeptide conformations from experimental distance constraints and energy minimization.
290.: Lee, K.H., Fitton, J.E. and Wüthrich, K. (1987) Biochim. Biophys. Acta 911, 144-153.
Nuclear magnetic resonance investigation of the conformation of d- haemolysin bound to dodecylphosphocholine micelles.
291.: Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go , N. and Wüthrich, K. (1987) J. Mol. Biol. 196, 611-639.
Protein structures in solution by nuclear magnetic resonance and distance geometry: the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.
292.: Vas/ ák, M., Wörgötter, E., Wagner, G., Kägi, J.H.R. and Wüthrich, K. (1987) J. Mol. Biol. 196, 711-719.
Metal coordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2.
293.: Chazin, W.J. and Wüthrich, K. (1987) J. Magn. Reson. 72, 358-363.
Optimization of homonuclear relayed coherence transfer experiments with proteins in H2O solution.
294.: Otting, G., Grütter, R., Leupin, W., Minganti, C., Ganesh, K.N., Sproat, B.S., Gait , M.J. and Wüthrich, K. (1987) Eur. J. Biochem. 166, 215-220.
Sequential NMR assignments of labile protons in DNA using two-dimensional nuclear Overhauser enhancement spectroscopy with three jump-and-return pulse sequences.
295.: Widmer, H. and Wüthrich, K. (1987) J. Magn. Reson. 74, 316-336.
Simulated two-dimensional NMR cross peak fine structures for 1H spin systems in polypeptides and polydeoxynucleotides.
296.: gner, G., Brühwiler, D. and Wüthrich, K. (1987) J. Mol. Biol. 196, 227-231.
Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance.
297.: Widmer, H., Wagner, G. and Wüthrich, K. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.)
pp. 498-499 , Schippert, Zürich.
Application of DQF-COSY, RELAYED-COSY and DOUBLE-RELAYED-COSY for the assignment of protein 1H-NMR spectra.
298.: Frey, M.H., Sørensen, O.W., Leupin, W., Denny, W.A., Rance, M., Ernst, R.R. and Wüthrich, K. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.) pp. 500-501, Schippert, Zürich.
Sequential resonance assignments of oligonucleotides with homonuclear and heteronuclear 2D NMR.
299.: Bodenhausen, G., Rance, M., Levitt, M.H., Sørensen, O.W., Meier, B.U., Pfändler, P., Denk, W., Wagner, G., Wüthrich, K. and Ernst, R.R. (1984) in Proceedings XXII Congress Ampère on Magnetic Resonance and Related Phenomena, (K.A. Müller, R. Kind and J. Roos, eds.) pp. 566-567, Schippert, Zürich.
New approaches to the measurement of cross-relaxation rates by two-dimensional NMR.
300.: Otting, G., Marchot, P., Bougis, P.E., Rochat, H. and Wüthrich, K. (1987) Eur. J. Biochem. 168, 603-607.
Monitoring the purification by high-performance liquid chromatography of cardiotoxins from Naja mossambica mossambica using phase-sensitive two-dimensional nuclear magnetic resonance.
301.: Otting, G., Steinmetz, W.E., Bougis, P.E., Rochat, H. and Wüthrich, K. (1987), Eur. J. Biochem. 168, 609-620.
Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica.
302.: Wang Q., Kline, A.D. and Wüthrich, K. (1987) Biochemistry 26, 6488-6493.
Amide proton exchange in the a-amylase polypeptide inhibitor Tendamistat studied by two-dimensional 1H nuclear magnetic resonance.
303.: Wüthrich, K. (1987) Optica Pura Y Aplicada 20, 145-151.
Nuclear magnetic resonance with proteins and nucleic acids.
304.: Wüthrich, K. (1987) in DNA-Protein Interactions and Gene Regulation, (E.B. Thompson and J. Papaconstantinou, eds.) pp. 87-94, University Press, Austin.
Nuclear magnetic resonance techniques for studies of protein-DNA interactions.
305.: Montelione, G.T., Wüthrich, K., Nice, E.C., Burgess, A.W. and Scheraga, H.A. (1987) Proc. Natl. Acad. Sci. USA 84, 5226-5230.
Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.
306.: Wörgötter, E., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1987) Eur. J. Biochem. 167, 457-466.
Sequence-specific 1H NMR assignments in rat liver metallothionein-2.
307.: Wagner, G., Frey, M.E., Neuhaus, D., Wörgötter, E., Braun, W., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1987) in Metallothionein II, (J.H.R. Kägi and Y. Kojima, eds.) Experientia Suppl. 52, 149-157.
Spatial structure of rabbit liver metallothionein-2 in solution by NMR.
308.: Wüthrich, K. (1987) Q. Rev. Biophys. 19, 3-5.
Nuclear magnetic resonance - from molecules to man.
309.: Wüthrich, K. (1987) Life Sci. Adv. Biochem. 6, 83-87.
Nuclear magnetic resonance with proteins and nucleic acids.
310.: Wörgötter, E., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Am. Chem. Soc. 110, 2388-2393.
Heteronuclear filters for two-dimensional 1H NMR: identification of the metal-bound amino acids in metallothionein and observation of small heteronuclear long-range couplings.
311.: Steinmetz, W.E., Bougis, P.E., Rochat, H., Redwine, O.D., Braun, W. and Wüthrich, K. (1988) Eur. J. Biochem. 172, 101-116.
1H nuclear magnetic resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins.
312.: Siekmann, J., Wenzel, H.R., Schröder, W., Schutt, H., Truscheit, E., Arens, A., Rauenbusch, E., Chazin, W.J., Wüthrich, K. and Tschesche, H. (1987) Biol. Chem. Hoppe-Seyler 368, 1589-1596.
Pyroglutamyl-aprotinin, a new aprotinin homologue from bovine lungs - isolation, properties, sequence analysis and characterization using 1H nuclear magnetic resonance in solution.
313.: Widmer, H., Wagner, G., Schweitz, H., Lazdunski, M. and Wüthrich, K. (1988) Eur. J. Biochem. 171, 177-192.
The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence-specific 1H NMR assignments.
314.: Otting, G. and Wüthrich, K. (1987) J. Magn. Reson. 75, 546-549.
Pre-TOCSY, a new experiment for obtaining complete 2D 1H NMR spectra of proteins in H2O solution.
315.: Arseniev, A., Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Mol. Biol. 201, 637-657.
Three-dimensional structure of rabbit liver [Cd7]-metallothionein-2a in aqueous solution determined by nuclear magnetic resonance.
316.: Otting, G. and Wüthrich, K. (1988) J. Magn. Reson. 76, 569-574 .
Efficient purging scheme for proton-detected heteronuclear two-dimensional NMR.
317.: Montelione, G.T., Wüthrich, K. and Scheraga, H.A. (1988) Biochemistry 27, 2235-2243.
Sequence-specific 1H NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor.
318.: Wüthrich, K. (1988) Physikalische Blätter 44, 103-109.
Proteinstrukturermittlung in Lösung mittels kernmagnetischer Resonanzspektroskopie.
319.: Celda, B., Widmer, H., Leupin, W., Chazin, W.J., Denny, W.A. and Wüthrich, K. (1989) Biochemistry 28, 1462-1471.
Conformational studies of d-(AAAAATTTTT)2 using constraints from nuclear Overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional 1H nuclear magnetic resonance spectra.
320.: Kline, A.D., Braun, W. and Wüthrich, K. (1988) J. Mol. Biol. 204, 675-724.
Determination of the complete three-dimensional structure of the a-amylase inhibitor Tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry.
321.: Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1988) J. Mol. Biol. 203, 251-268.
Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy.
322.: Grütter, R., Otting, G., Wüthrich, K. and Leupin, W. (1988) Eur. Biophys. J. 16, 279-286.
OR3 operator of bacteriophage l in a 23 base-pair DNA fragment: sequence-specific
1H NMR assignments for the non-labile protons and comparison with the isolated 17 base-pair operator.
323.: Wüthrich, K. (1988) in Water and Ions in Biological Systems, (P. Läuger, L. Packer and V. Vasilescu, eds.) pp. 33-41, Birkhäuser, Basel.
Protein molecules in aqueous solution viewed by nuclear magnetic resonance.
324.: Wüthrich, K. (1988) GIT Fachz. Lab. 5, 481-488.
Dreidimensionale Proteinstrukturen in Lösung.
325.: Wüthrich, K. (1988) in NMR Spectroscopy in Drug Research, (J.W. Jaroszewski, K. Schaumburg and H. Kofod, eds.) pp. 194-208, Munksgaard, Copenhagen.
Three-dimensional protein structures in solution viewed by NMR.
326.: Labhardt, A.M., Hunziker-Kwik, E.H. and Wüthrich, K. (1988) Eur. J. Biochem. 177,
295-305.
Secondary structure determination for a-neurotoxin from Dendroaspis polylepis based on sequence-specific 1H-nuclear-magnetic-resonance assignments.
327.: Martin, E., Bösch, C., Duc, G., Wüthrich, K., Brunner, P. and Fanconi, A. (1988) Helv. paediat. Acta 43, 53-74.
Magnetresonanz in der pädiatrischen Forschung und Klinik. I. Teil: Was können wir von dieser neuen Methode erwarten?
328.: Griesinger, C., Otting, G., Wüthrich, K. and Ernst, R.R. (1988) J. Am. Chem. Soc. 110, 7870-7872.
Clean-TOCSY for 1H spin system identification in macromolecules.
329.: Müller, M., Affolter, M., Leupin, W., Otting, G., Wüthrich, K. and Gehring, W.J. (1988) EMBO J. 7, 4299-4304.
Isolation and sequence-specific DNA binding of the Antennapedia homeodomain.
330.: Otting, G., Qian, Y.Q., Müller, M., Affolter, M., Gehring, W.J. and Wüthrich, K. (1988) EMBO J. 7, 4305-4309.
Secondary structure determination for the Antennapedia homeodomain by nuclear magnetic resonance and evidence for a helix-turn-helix motif.
331.: Wüthrich, K. (1988) in Protein Structure and Protein Engineering, 39 Colloquium Mosbach (E.L. Winnacker and R. Huber, eds.) pp. 37- 44, Springer, Heidelberg.
The method of protein structure determination by NMR in solution: initial new insights relating to molecular mobility.
332.: Wüthrich, K. (1989) Science 243, 45-50.
Protein structure determination in solution by nuclear magnetic resonance spectroscopy.
333.: Wüthrich, K. (1989) Acc. Chem. Res. 22, 36-44.
The development of nuclear magnetic resonance spectroscopy as a technique for protein structure determination.
334.: Otting, G. and Wüthrich, K. (1989) J. Am. Chem. Soc. 111, 1871-1875.
Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules.
335.: Billeter, M., Kline, A.D., Braun, W., Huber, R and Wüthrich, K. (1989) J. Mol. Biol. 206, 677-687.
Comparison of the high-resolution structures of the a-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals.
336.: Braun, W., Epp, O., Wüthrich, K. and Huber, R. (1989) J. Mol. Biol. 206, 669-676.
Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial model.
337.: Haruyama, H. and Wüthrich, K. (1989) Biochemistry 28, 4301-4312.
Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance.
338.: Haruyama, H., Qian, Y.Q. and Wüthrich, K. (1989) Biochemistry 28, 4312-4317.
Static and transient hydrogen-bonding interactions in recombinant desulfatohirudin studied by 1H nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts.
339.: Güntert, P., Braun, W., Billeter, M. and Wüthrich, K. (1989) J. Am. Chem. Soc. 111, 3997-4004.
Automated stereospecific 1H NMR assignments and their impact on the precision of protein structure determinations in solution.
340.: Senn, H., Werner, B., Messerle, B.A., Weber, C., Traber, R. and Wüthrich, K. (1989) FEBS Lett. 249, 113-118.
Stereospecific assignment of the methyl 1H NMR lines of valine and leucine in polypeptides by nonrandom 13C labelling.
341.: Schaumann, T., Braun, W. and Wüthrich, K. (1990) Biopolymers 29, 679-694.
The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space.
342.: Billeter, M., Schaumann, T., Braun, W. and Wüthrich, K. (1990) Biopolymers 29, 695-706.
Restrained energy refinement with two different algorithms and force fields of the structure of the a-amylase inhibitor tendamistat determined by NMR in solution.
343.: Bösch, C., Grütter, R., Martin, E., Duc, G. and Wüthrich, K. (1989) Radiology 172,
197-199.
Variations in the in vivo P-31 MR spectra of the developing human brain during postnatal life.
344.: Neri, D., Szyperski, T., Otting, G., Senn, H. and Wüthrich, K. (1989) Biochemistry 28, 7510-7516.
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 13C labeling.
345.: Wüthrich, K. (1988) in Proceedings of the 8th International Biotechnology Symposium, (G. Durand, L. Bobichon and J. Florent, eds.) pp. 270-278, Société Française de Microbiologie, Paris.
Protein structure determination by nuclear magnetic resonance in solution.
346.: Billeter, M. and Wüthrich, K. ((1989) in Computer-Aided Molecular Design, (W.G. Richards, ed.) pp. 197-201, IBC Technical Services Ltd., Oxford.
Interactive computer graphics for the determination of biopolymer conformations from NMR data measured in solution.
347.: Qian, Y.Q., Billeter, M., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1989) Cell 59, 573-580.
The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors.
348.: Widmer, H., Billeter, M. and Wüthrich, K. (1989) Proteins 6, 357-371.
Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy.
349.: Wider, G., Neri, D., Otting, G. and Wüthrich, K. (1989) J. Magn. Reson. 85, 426-431.
A heteronuclear three-dimensional NMR experiment for measurements of small heteronuclear coupling constants in biological macromolecules.
350.: Wüthrich, K. (1989) Chemica Scripta 29A, 23-26.
Three-dimensional structures of non-crystalline proteins observed by nuclear magnetic resonance.
351.: Otting, G. and Wüthrich, K. (1989) J. Magn. Reson. 85, 586-594.
Extended heteronuclear editing of 2D 1H NMR spectra of isotope-labeled proteins, using the X(w1,w2)-double-half-filter.
352.: Neri, D., Otting, G. and Wüthrich, K. (1990) Tetrahedron 46, 3287-3296.
1H and 13C NMR chemical shifts of the diastereotopic methyl groups of valyl and leucyl residues in peptides and proteins.
353.: Messerle, B.A., Wider, G., Otting, G., Weber, C. and Wüthrich, K. (1989) J. Magn. Reson. 85, 608-613.
Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with H2O solutions.
354.: Otting, G. and Wüthrich, K. (1990) Q. Rev. Biophys. 23, 39-96.
Heteronuclear filters in two-dimensional [1H,1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions.
355.: Billeter, M., Qian, Y.Q., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1990) J. Mol. Biol. 214, 183-197.
Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy.
356.: Messerle, B.A., Schäffer, A., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1990)J. Mol. Biol. 214, 765-779.
Three-dimensional structure of human [113Cd7]-metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.
357.: Messerle, B.A., Bos, M., Schäffer, A., Va/s ák, M., Kägi, J.H.R. and Wüthrich, K. (1990) J. Mol. Biol. 214, 781-786.
Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy.
358.: Wüthrich, K. (1989) Methods in Enzymology 177, 125-131.
Determination of three-dimensional protein structures in solution by nuclear magnetic resonance: an overview.
359.: Otting, G. and Wüthrich, K. (1990) in Water and Ions in Biomolecular Systems (D. Vasilescu, J. Jaz, L. Packer, B. Pullman, eds.) pp. 141-147, Birkhäuser, Basel.
Studies of protein hydration by direct NMR observation of individual protein-bound water molecules.
360.: Neri, D., Otting, G. and Wüthrich, K. (1990) J. Am. Chem. Soc. 112, 3663-3665.
New nuclear magnetic resonance experiment for measurements of the vicinal coupling constants 3JHNa in proteins.
361.: Leupin, W., Otting, G., Amacker, H. and Wüthrich, K. (1990) FEBS Lett. 263, 313-316.
Application of 13C(wl )-half-filtered [1H,1H]-NOESY for studies of a complex formed between DNA and a 13C-labeled minor-groove-binding drug.
362.: Wüthrich, K. (1990) Biochem. Pharmacol. 40, 55-62.
Structure and dynamics in proteins of pharmacological interest.
363.: Wüthrich, K. (1989) in Protein Structure and Engineering, (O. Jardetzky, ed.) NATO ASI Series: Life Sciences A183, 69-78.
NMR method for protein structure determination in solution.
364.: Grütter, R., Bösch, Ch., Müri, M., Martin, E. and Wüthrich, K. (1990) Magn. Reson. in Medicine 15, 128-134.
A simple design for a double-tunable probe head for imaging and spectroscopy at high fields.
365.: Otting, G., Orbons, L.P.M. and Wüthrich, K. (1990) J. Magn. Reson. 89, 423-430.
Suppression of zero-quantum coherence in NOESY and soft-NOESY.
366.: Vendrell, J., Wider, G., Avilés, F.X. and Wüthrich, K. (1990) Biochemistry 29, 7515-7522.
Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
367.: Gehring, W.J., Müller, M., Affolter, M., Percival-Smith, A., Billeter, M., Qian, Y.Q., Otting, G. and Wüthrich, K. (1990) Trends in Genetics 6, 323-329.
The structure of the homeodomain and its functional implications.
368.: Otting, G., Qian, Y.Q., Billeter, M., Müller, M., Affolter, M., Gehring, W.J. and Wüthrich, K. (1990) EMBO J. 9, 3085-3092.
Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution.
369.: Wüthrich, K. (1990) Current Science 59, 825-31.
The Ramachandran plot and the NMR method for protein structure determination.
370.: Wider, G., Weber, C., Traber, R., Widmer, H. and Wüthrich, K. (1990) J. Am. Chem. Soc. 112, 9015-016.
Use of a double-half-filter in two-dimensional 1H nuclear magnetic resonance studies of receptor-bound cyclosporin.
371.: Wüthrich, K. (1990) J. Biol. Chem. 265, 22059-22062 .
Protein structure determination in solution by NMR spectroscopy.
372.: Vendrell, J., Billeter, M., Wider, G., Avilés, F.X. and Wüthrich, K. (1991) EMBO J. 10, 11-15.
The NMR structure of the activation domain isolated from porcine
procarboxypeptidase B.
373.: Grütter, R., Bösch, C., Martin, E. and Wüthrich, K. (1990) NMR in Biomedicine 3, 265-271.
A method for rapid evaluation of saturation factors in in vivo surface coil NMR spectroscopy using B1-insensitive pulse cycles.
374.: Güntert, P., Braun, W. and Wüthrich, K. (1991) J. Mol. Biol. 217, 517-530.
Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.
375.: Güntert, P., Qian, Y.Q., Otting, G., Müller, M., Gehring, W.J. and Wüthrich, K. (1991) J. Mol. Biol. 217, 531-540.
Structure determination of the Antp (C39->S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA.
376.: Affolter, M., Percival-Smith, A., Müller, M., Billeter, M., Qian, Y.Q., Otting, G., Wüthrich, K. and Gehring, W.J. (1991) Cell 64, 879-880.
Similarities between the homeodomain and the hin recombinase DNA-binding domain.
377.: Wüthrich, K. (1991) 309 pages (Kagaku Dozin, Tokyo, Japan).
378.: Wider, G., Neri, D. and Wüthrich, K. (1991) J. Biomol. NMR 1, 93-98.
Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment.
379.: Chary, K.V.R., Otting, G. and Wüthrich, K. (1991) J. Magn. Reson. 93, 218-224.
Measurement of small heteronuclear 1H-15N coupling constants in 15N-labeled proteins by 3D HNNHAB-COSY".
380.: Weber, C., Wider, G., von Freyberg, B., Traber, R., Braun, W., Widmer, H. and Wüthrich, K. (1991) Biochemistry 30, 6563-6574.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
381.: Otting, G., Liepinsh, E. and Wüthrich, K. (1991) J. Am. Chem. Soc. 113, 4363-4364.
Proton exchange with internal water molecules in the protein BPTI in aqueous solution.
382.: Wider, G., Weber, C. and Wüthrich, K. (1991) J. Am. Chem. Soc. 113, 4676-4678.
Proton-proton Overhauser effects of receptor-bound cyclosporin A observed with the use of a heteronuclear-resolved half-filter experiment.
383.: Wüthrich, K. (1991) in Proteins, Structure, Dynamics and Design (V. Renugopalakrishnan, P.R. Carey, I.C.P. Smith, S.G. Huang, A.C. Storer, eds.) pp. 3-10, ESCOM, Leiden.
NMR structures of proteins: Improved precision through stereospecific resonance assignments.
384.: Eccles, C., Güntert, P., Billeter, M. and Wüthrich, K. (1991) J. Biomol. NMR 1, 111-130.
Efficient analysis of protein 2D NMR spectra using the software package EASY.
385.: Neri, D., Billeter, M. and Wüthrich, K. (1992) J. Mol. Biol. 223, 743-767.
Determination of the NMR solution structure of the DNA-binding domain 1-69 of the 434 repressor and comparison with the X-ray crystal structure.
386.: Otting, G., Liepinsh, E., Farmer II, B.T. and Wüthrich, K. (1991) J. Biomol. NMR 1,
209-215.
Protein hydration studied with homonuclear 3D 1H NMR experiments.
387.: Wüthrich, K., Spitzfaden, C., Memmert, K., Widmer, H. and Wider, G. (1991) FEBS Lett. 285, 237-247.
Protein secondary structure determination by NMR: application with recombinant human cyclophilin.
388.: Sodano, P., Chary, K.V.R., Björnberg, O., Holmgren, A., Kren, B., Fuchs, J.A. and Wüthrich, K. (1991) Eur. J. Biochem. 200, 369-377.
Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin: sequence-specific assignments and secondary structure determination of the oxidized form.
389.: Kallen, J., Spitzfaden, C., Zurini, M.G.M., Wider, G., Widmer, H., Wüthrich, K. and Walkinshaw, M.D. (1991) Nature 353, 276-279.
Structure of human cyclophilin and its binding site for cyclosporin A determined by
X-ray crystallography and NMR spectroscopy.
390.: Mertz, J.E., Güntert, P., Wüthrich, K. and Braun, W. (1991) J. Biomol. NMR 1, 257-269.
Complete relaxation matrix refinement of NMR structures of proteins using analytically calculated dihedral angle derivatives of NOE intensities.
391.: Wüthrich, K. (1991) in Protein Conformation, Ciba Foundation Symposium 161, pp.
136-149, Wiley, Chichester.
Six years of protein structure determination by NMR spectroscopy: What have we learned?
392.: Sodano, P., Xia, T., Bushweller, J.H., Björnberg, O., Holmgren, A., Billeter , M. and Wüthrich, K. (1991) J. Mol. Biol. 221, 1311-1324.
Sequence-specific 1H NMR assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.
393.: Wüthrich, K., v. Freyberg, B., Weber, C., Wider, G., Traber, R., Widmer, H. and Braun, W. (1991) Science 254, 953-954.
Receptor-induced conformation change of the immunosuppressant cyclosporin A.
394.: Otting, G., Liepinsh, E. and Wüthrich, K. (1991) Science 254, 974-980.
Protein hydration in aqueous solution.
395.: Güntert, P. and Wüthrich, K. (1991) J. Biomol. NMR 1, 447-456.
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
396.: Billeter, M., Vendrell, J., Wider, G., Avilés, F.X., Coll, M., Guasch, A., Huber , R. and Wüthrich, K. (1992) J. Biomol. NMR 2, 1-10.
Comparison of the NMR solution structure with the X-ray crystal structure of the activation domain from procarboxypeptidase B.
397.: Montelione, G.T., Wüthrich, K., Burgess, A.W., Nice, E.C., Wagner, G., Gibson, D. and Scheraga, H.A. (1992) Biochemistry 31, 236-249.
Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.
398.: Wüthrich, K. (1991) Methods in Enzymology 205, 502-520.
Determination of the three-dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution.
399.: Spitzfaden, C., Weber, H.P., Braun, W., Kallen, J., Wider, G., Widmer, H., Walkinshaw, M.D. and Wüthrich, K. (1992) FEBS Lett. 300, 291-300.
Cyclosporin A-cyclophilin complex formation. A model based on X-ray and NMR data.
400.: Wüthrich, K. and Otting, G. (1992) Int. J. Quant. Chem. 42, 1553-1561.
Studies of protein hydration in aqueous solution by high-resolution nuclear magnetic resonance spectroscopy.
401.: Otting, G., Liepinsh , E. and Wüthrich, K. (1992) J. Am. Chem. Soc. 114, 7093-7095.
Polypeptide hydration in mixed solvents at low temperatures.
402.: Güntert, P. and Wüthrich, K., (1992) J. Magn. Reson. 96, 403-407.
FLATTæA new procedure for high-quality baseline correction of multidimensional NMR spectra.
403.: Neri, D., Wider, G. and Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 4397-4401.
Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage
434 repressor in the urea-unfolded form.
404.: Xia, T., Bushweller, J.H., Sodano, P., Billeter, M., Björnberg, O., Holmgren, A. and
Wüthrich, K. (1992) Protein Science 1, 310-321.
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
405.: Billeter, M., Neri, D., Otting, G., Qian, Y.Q. and Wüthrich, K., (1992) J. Biomol. NMR 2, 257-274.
Precise vicinal coupling constants 3JHNa in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments.
406.: Neri, D., Wider , G. and Wüthrich, K. (1992) FEBS Lett. 303, 129-135.
1H, 15N and 13C NMR assignments of the 434 repressor fragments 1-63 and 44-64 unfolded in 7 M urea.
407.: Messerle, B.A., Schäffer, A., Vas/ ák, M., Kägi, J.H.R. and Wüthrich, K. (1992) J. Mol. Biol. 225, 433-443.
Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy.
408.: Szyperski, T., Neri, D., Leiting, B., Otting, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 323-334.
Support of 1H NMR assignments in proteins by biosynthetically directed fractional
13C-labeling.
409.: Liepinsh, E., Otting, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 447-465.
NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.
410.: Vendrell, J., Guasch, A., Coll, M., Villegas, V. Billeter, M., Wider, G., Huber, R., Wüthrich, K. and Avilés, F. (1992) Biol. Chem. Hoppe-Seyler 373, 387-392.
Pancreatic procarboxypeptidases: their activation processes related to the structural features of the zymogens and activation segments.
411.: Berndt, K.D., Güntert, P., Orbons, L.P.M. and Wüthrich, K. (1992) J. Mol. Biol. 227, 757-775.
Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures.
412.: Szyperski, T., Güntert, P., Otting, G. and Wüthrich, K. (1992) J. Magn. Reson. 99, 552-560.
Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets.
413.: Bushweller, J.H., Åslund, F., Wüthrich, K. and Holmgren, A. (1992) Biochemistry 31,
928-293 .
Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14ÆS) and its mixed disulfide with glutathione.
414.: Brown, L.R. and Wüthrich, K. (1992) J. Mol. Biol. 227, 1118-1135.
Nuclear magnetic resonance solution structure of the a-neurotoxin from the black mamba (Dendroaspis polylepis polylepis).
415.: Neri, D., Billeter, M., Wider, G. and Wüthrich, K. (1992) Science 257, 1559-1563.
NMR determination of residual structure in a urea-denatured protein, the 434 repressor.
416.: Wüthrich, K., Szyperski, T., Leiting, B. and Otting, G., (1992) in Frontiers and New Horizons in Amino Acid Research (Proc. 1st Biennial International Conference on Amino Acid Research, Frontiers and Horizons, K. Takai, ed.), pp.41-48, Elsevier, Amsterdam.
Biosynthetic pathways of the common proteinogenic amino acids investigated by fractional 13C labeling and NMR spectroscopy.
417.: Wüthrich, K., Otting, G. and Liepinsh, E. (1992) Faraday Discuss. 93, 35-45.
Protein hydration in aqueous solution.
418.: Braun, W., Vas/ ák, M., Robbins, A.H., Stout, C.D., Wagner, G., Kägi, J.H.R. and
Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 10124-10128.
Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2.
419.: Qian, Y.Q., Otting, G., Furukubo-Tokunaga, K., Affolter, M., Gehring, W.J. and
Wüthrich, K. (1992) Proc. Natl. Acad. Sci. USA 89, 10738-10742.
NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein.
420.: Güntert, P., Dötsch, V., Wider, G. and Wüthrich, K. (1992) J. Biomol. NMR 2, 619-629.
Processing of multi-dimensional NMR data with the new software PROSA.
421.: Liepinsh, E., Otting, G. and Wüthrich, K. (1992) Nucl. Acids Res. 20, 6549-6553.
NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.
422.: Szyperski, T. Güntert, P., Stone, S.R. and Wüthrich, K. (1992) J. Mol. Biol. 228, 1193-1205.
Nuclear magnetic resonance solution structure of hirudin(1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain.
423.: Szyperski, T., Güntert, P., Stone, S.R., Tulinsky, A., Bode, W., Huber, R. and Wüthrich, K. (1992) J. Mol. Biol. 228, 1206-1211.
Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin(1-51).
424.: Wüthrich, K. (1992) Nova acta Leopoldina NF 60, Nr. 266, 47-56.
Strukturermittlung an Proteinen und Nukleinsäuren in Lösung mittels NMR.
425.: Wüthrich, K. and Gehring, W.J. (1992) in Transcriptional Regulation (S.L. McKnight and K.R. Yamamoto, eds.) pp. 535-577, Cold Spring Harbor Laboratory Press, Plainview, NY, USA.
Transcriptional regulation by homeodomain proteins: structural, functional, and genetic aspects.
426.: Szyperski, T., Wider, G., Bushweller, J.H. and Wüthrich, K. (1993) J. Biomol. NMR 3,
127-132.
3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins.
427.: Qian, Y.Q., Otting, G. and Wüthrich, K. (1993) J. Am. Chem. Soc. 115, 1189-1190.
NMR detection of hydration water in the intermolecular interface of a protein-DNA complex.
428.: Wüthrich, K., Otting, G., Qian, Y.Q., Billeter, M. and Gehring, W. (1992) in Molecular Structure and Life (Y. Kyogoku and Y. Nishimura, eds.), pp.115-127, Japan Scientific Societies Press, Tokyo.
Molecular recognition in the homeodomain-DNA system.
429.: Güntert, P., Schaefer, N., Otting, G. and Wüthrich, K. (1993) J. Magn. Reson. 101, 103-105.
POMA: A complete Mathematica implementation of the NMR product-operator formalism.
430.: Leiting, B., de Francesco, R., Tomei, L., Cortese, R., Otting, G. and Wüthrich, K. (1993) EMBO J. 12, 1797-1803.
The three-dimensional NMR-solution structure of the polypeptide fragment 195-286 of the LFB1/HNF1 transcription factor from rat liver comprises a non-classical homeodomain.
431.: Brown, L.R., Mronga, S., Bradshaw, R.A., Ortenzi, C., Luporini, P. and Wüthrich, K. (1993) J. Mol. Biol. 231, 800-816.
Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi.
432.: Berndt, K.D., Beunink, J., Schröder, W. and Wüthrich, K. (1993) Biochemistry 32,
4564-4570.
Designed replacement of an internal hydration water molecule in BPTI: structural and functional implications of a Gly-to-Ser mutation.
433.: Otting, G., Liepinsh, E. and Wüthrich, K. (1993) Biochemistry 32, 3571-3582.
Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.
434.: Szyperski, T., Luginbühl, P., Otting, G., Güntert, P. and Wüthrich, K. (1993) J. Biomol. NMR 3, 151-164.
Protein dynamics studied by rotating frame 15N spin relaxation times.
435.: Liepinsh, E., Rink, H., Otting, G. and Wüthrich, K. (1993) J. Biomol. NMR 3, 253-257.
Contribution from hydration of carboxylate groups to the spectrum of water-polypeptide proton-proton Overhauser effects in aqueous solution.
436.: Gehring, W.J. and Wüthrich, K. (1993) Structure 0, IV-V .
Structural and functional analysis of homeodomain-DNA interactions.
437.: Antuch, W., Berndt, K.D., Chavez, M.A., Delfin, J. and Wüthrich, K. (1993) Eur. J. Biochem. 212, 675-684.
The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus.
438.: O'Connell, J.F., Bougis, P.E. and Wüthrich, K. (1993) Eur. J. Biochem. 213, 891-900.
Determination of the nuclear-magnetic-resonance solution structure of cardiotoxin
CTX IIb from Naja mossambica mossambica.
439.: Wüthrich, K., Güntert, P. and Berndt, K.D. (1993) in Innovations in Proteases and their Inhibitors (F.X. Avilés, ed.) pp. 407-424, Walter de Gruyter, Berlin.
Computer-supported NMR structure determination of proteins in solution illustrated with studies of protein proteinase inhibitors.
440.: Berndt, K.D., Güntert, P. and Wüthrich, K. (1993) J. Mol. Biol. 234, 735-750.
Nuclear magnetic resonance solution structure of dendrotoxin K from the venom of Dendroaspis polylepis polylepis.
441.: an, Y.Q., Otting, G., Billeter, M., Müller, M., Gehring, W.J. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1070-1083.
Nuclear magnetic resonance spectroscopy of a DNA complex with the uniformly 13C-labeled Antennapedia homeodomain and structure determination of the DNA-bound homeodomain.
442.: Billeter, M., Qian, Y.Q., Otting, G., Müller, M. Gehring, W. J. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1084-1093.
Determination of the nuclear magnetic resonance solution structure of an Antennapedia homeodomain-DNA complex.
443.: Billeter, M. and Wüthrich, K. (1993) J. Mol. Biol. 234, 1094-1097.
Model Studies relating nuclear magnetic resonance data with the three-dimensional structure of protein-DNA complexes.
444.: Brunne, R.M., Liepinsh, E., Otting, G., Wüthrich, K. and van Gunsteren, W.F. (1993)
J. Mol. Biol. 231, 1040-1048.
Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations.
445.: Güntert, P., Berndt, K.D. and Wüthrich, K. (1993) J. Biomol. NMR 3, 601-606.
The program ASNO for computer-supported collection of NOE upper distance constraints as input for protein structure determination.
446.: Wider, G. and Wüthrich, K. (1993) J. Magn. Reson. B 102, 239-241.
A simple experimental scheme using pulsed field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra.
447.: Fede, A., Billeter, M., Leupin, W. and Wüthrich, K. (1993) Structure 1, 177-186.
Determination of the NMR solution structure of the Hoechst 33258-d(GTGGAATTCCAC)2 complex and comparison with the X-ray crystal structure.
448.: Szyperski, T., Scheek, S., Johansson, J., Assmann, G., Seedorf, U. and Wüthrich, K. (1993) FEBS Lett. 335, 18-26.
NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2.
449.: Szyperski, T., Wider, G. Bushweller, J.H. and Wüthrich, K. (1993) J. Am. Chem. Soc. 115, 9307-9308.
Reduced dimensionality in triple-resonance NMR experiments.
450.: Wüthrich, K. (1993) in Molecular Structures in Biology (R. Diamond, T.F. Koetzle, K. Prout, J.S. Richarsdon, eds.) pp. 20-26, Oxford Univ. Press, Oxford.
Biopolymers: an NMR survey.
451.: Otting, G., Billeter, M., Wüthrich, K., Roth, H.J., Leumann, C. and Eschenmoser, A. (1993) Helv. Chim. Acta 76, 2701-2756.
Warum Pentose- und nicht Hexose-Nucleinsäuren? `Homo-DNS': 1H-, 13C-, 31P- und 15N-NMR-spektroskopische Untersuchung von ddGlc(A-A-A-A-A-T-T-T-T-T) in wässriger Lösung
452.: Bushweller, J.H., Holmgren, A. and Wüthrich, K. (1993) Eur. J. Biochem. 218, 327-334.
Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
453.: Wüthrich, K. (1994) Current Opinion in Structural Biology 4, 93-99.
NMR assignment as a basis for structural characterization of denatured states of globular proteins.
454.: Sevilla-Sierra, P., Otting, G. and Wüthrich, K. (1994) J. Mol. Biol. 235, 1003-1020.
Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor.
455.: Wüthrich, K. (1993) Les Cahiers de la Fondation, Vol. 8, Fondation Louis Jeantet de Médecine, Genève, Suisse.
Three-dimensional protein structures in biological and biomedical research.
456.: Bushweller, J.H., Billeter, M., Holmgren, A. and Wüthrich, K. (1994) J. Mol. Biol. 235, 1585-1597.
The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.
457.: Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K. and Plückthun, A. (1994) Nature 368, 261-265.
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.abstract
458.: O'Connell, J.F., Bender, R., Engels, J.W., Koller, K.P., Scharf, M. and Wüthrich, K. (1994) Eur. J. Biochem. 220, 763-770.
The nuclear-magnetic-resonance solution structure of the mutant a-amylase inhibitor [R19L]Tendamistat and comparison with wild-type Tendamistat.
459.: Leupin, W., Bur, D., Dorn, A., Ji, Y.H., Labhardt, A., Fede, A., Billeter, M. and Wüthrich, K. (1994) Actual. Chim. Thér. 21, 153-170.
Bis-benzimidazole derivatives as DNA ligands: design based on the solution structure of a Hoechst 33258-DNA complex with subsequent molecular modelling.
460.: Wüthrich, K. (1994) in Toward a Molecular Basis of Alcohol Use and Abuse (B. Jansson, H. Jörnvall, U. Rydberg, L. Terenius, B.L. Vallee, eds.) pp. 261-268, Birkhäuser Verlag, Basel.
NMR, alcohols, protein solvation and protein denaturation.
461.: Qian, Y.Q. , Furukubo-Tokunaga, K., Resendez-Perez, D., Müller, M., Gehring, W.J. and Wüthrich K. (1994) J. Mol. Biol. 238, 333-345.
Nuclear magnetic resonance solution structure of the fushi tarazu homeodomain from Drosophila and comparison with the Antennapedia homoedomain.
462.: Qian, Y.Q., Resendez-Perez, D., Gehring, W.J. and Wüthrich, K. (1994) Proc. Natl. Acad. Sci. USA 91, 4091-4095.
The des(1-6)Antennapedia homeodomain: comparison of the NMR solution structure and the DNA-binding affinity with the intact Antennapedia homeodomain.
463.: Wüthrich, K. (1993) in DNA and Chromosomes, Cold Spring Harbor Symposia on Quantitative Biology 58, 149-157.
Hydration of biological macromolecules in solution: surface structure and molecular recognition.
464.: Johansson, J., Szyperski, T., Curstedt, T. and Wüthrich, K. (1994) Biochemistry 33, 6015-6023.
The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich a-helix.
465.: Wider, G., Dötsch, V. and Wüthrich, K. (1994) J. Magn. Reson. A 108, 255-258.
Self-compensating pulsed magnetic-field gradients for short recovery times.
466.: Spitzfaden, C., Braun, W., Wider, G., Widmer, H. and Wüthrich K. (1994) J. Biomol. NMR 4, 463-482.
Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex.
467.: Szyperski, T., Antuch, W., Schick, M., Betz, A., Stone, S.R. and Wüthrich, K. (1994) Biochemistry 33, 9303-9310.
Transient hydrogen bonds identified on the surface of the NMR solution structure of hirudin.
468.: Ottiger, M., Szyperski, T., Luginbühl, L., Ortenzi, C., Luporini, P., Bradshaw, R.A. and Wüthrich, K. (1994) Protein Science 3, 1515-1526.
The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi. abstract
469.: Mronga, S., Luginbühl, P., Brown, L.R., Ortenzi, C., Luporini, P., Bradshaw R.A. and Wüthrich, K. (1994) Protein Science 3, 1527-1536.
The NMR solution structure of the pheromone Er-1 from the ciliated protozoan Euplotes raikovi.
470.: Luginbühl, P., Ottiger, M., Mronga, S. and Wüthrich, K. (1994) Protein Science 3, 1537-1546.
Structure comparison of the pheromones Er-1, Er-10, and Er-2 from Euplotes raikovi.abstract
471.: Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. and Wüthrich, K. (1994) FEBS Lett. 352, 251-257.
NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor XA inhibitor from the tick Ornithodoros moubata.
472.: Szyperski, T., Pellecchia, M., Wall, D., Georgopoulos, C. and Wüthrich, K. (1994) Proc. Natl. Acad. Sci. USA 91, 11343-11347.
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region 2-108 comprising the highly conserved J-domain.
473.: Gehring, W.J., Qian, Y.Q., Billeter, M., Furukubo-Tokunaga, K., Schier, A. F., Resendez-Perez, D., Affolter, M., Otting, G. and Wüthrich, K. (1994) Cell 78, 211-223.
Homeodomain-DNA recognition.
474.: Dötsch, V., Wider, G. and Wüthrich, K. (1994) J. Magn. Reson. A 109, 263-264.
Phase-sensitive spectra in a single scan with coherence selection by pulsed field gradients.
475.: Schiffer, C.A., Huber, R., Wüthrich, K. and van Gunsteren, W.F. (1994) J. Mol. Biol. 241, 588-599.
Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals.
476.: Braun, D., Wider, G. and Wüthrich, K. (1994) J. Am. Chem. Soc. 116, 8466-8469.
Sequence-corrected 15N ``Random Coil'' chemical shifts.
477.: Szyperski, T., Pellecchia, M. and Wüthrich, K. (1994) J. Magn. Reson. B 105, 188-191.
3D Ha/bCa/b(CO)NHN, a projected 4D NMR experiment for sequential correlation of polypeptide 1Ha/b, 13Ca/b and backbone 15N and 1HN chemical shifts.
478.: Bartels, C. and Wüthrich, K. (1994) J. Biomol. NMR 4, 775-785.
A spectral correlation function for efficient sequential NMR assignments of uniformly 15N-labeled proteins.
479.: Altschuh, D., Braun, W., Kallen, J., Mikol, V., Spitzfaden, C., Thierry, J.C., Vix, O., Walkinshaw, M.D. and Wüthrich, K. (1994) Structure 10, 963-972.
Conformational polymorphism of cyclosporin A.
480.: Smith, P.E., van Schaik, R.C., Szyperski, T., Wüthrich, K. and van Gunsteren, W.F. (1995) J. Mol. Biol. 246, 356-365.
Internal mobility of the basic pancreatic trypsin inhibitor in solution: A comparison of NMR spin relaxation measurements and molecular dynamics simulations.
481.: Braun, W., Kallen, J., Mikol, V., Walkinshaw, M.D. and Wüthrich K. (1995) FASEB Journal 9, 63-72.
Three-dimensional structure and actions of immunosuppressants and their immunophilins.
482.: Johansson, J., Szyperski, T. and Wüthrich, K. (1995) FEBS Lett. 362, 261-265.
Pulmonary surfactant-associated polypeptide SP-C in lipid micelles: CD studies of intact SP-C and NMR secondary structure determination of depalmitoyl-SP-C(1-17).
483.: Wüthrich, K. (1995) Acta Cryst. D 51, 249-270.
NMR-this other method for protein and nucleic acid structure determination.
484.: Wüthrich, K. (1995) in Proceedings of the XIIIth International Symposium on Medical Chemistry (J.-C. Muller, ed.) Eur. J. Med. Chem. 30, 68s-84s.
Structure determination of biological macromolecules by NMR in solution: Impact in biomedical research.
485.: Dötsch, V., Wider, G., Siegal, G. and Wüthrich, K. (1995) FEBS Lett. 366, 6-10.
Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor.
486.: Wüthrich, K. (1995) NMR in structural biology - A collection of papers by Kurt Wüthrich, 738 pages, World Scientific, Singapore.
487.: Szypersky, T., Braun, D., Fernández, C., Bartels, C. and Wüthrich K. (1995) J. Magn. Reson. B 108, 197-203.
A novel reduced-dimensionality triple-resonance experiment for efficient polypeptide backbone assignment, 3D CO HN N CA.
488.: Bartels, C., Xia, T., Billeter, M., Güntert, P. and Wüthrich K. (1995) J. Biol. NMR 6, 1-10.
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.
489.: Dötsch, V., Wider, G., Siegal, G. and Wüthrich, K. (1995) FEBS Lett. 372, 288-290.
Salt-stabilized globular protein structure in 7M aqueous ureal solution.
490.: Brunne, R.M., Berndt, K.D., Güntert, P., Wüthrich, K. and van Gunsteren, W.F. (1995) Proteins 1, 49-62.
Structure and internal dynam