References 1963 - 1979

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 Kernresonanzspek-troskopie.

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 P450_cam 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 Protein (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. 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, –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 V^II4 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. Vašák, 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) Japanese Edition of 'NMR in Biological Research: Peptides and Proteins' (Translation by Y. Arata and M. Kainosho). Kagaku Dozin, Tokyo, Japan.