References 1980 - 1989
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., Gō , 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 3Jin 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 C–C 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 fromEscherichia 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 aeruginosaferrocytochrome c 551 by 1H NMR.
228. Wüthrich, K., Strǒp, 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 helix than from antiparallel sheets.
229. Rance, M., Wagner, G., Sørensen, O.W., Wüthrich, K. and Ernst, R.R. (1984) J. Magn. Reson. 59, 250–261.
Applications of -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., Vašák, 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 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 -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–C proton coupling constants, 3JHN , in a globular protein: use of 3JHN 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 -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., Vašák, 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., Vašák, 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., Vašák, 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., Vašák, 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., Vašák, 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 -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, 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 -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 -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 Membrane, 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 - 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. Vašák, 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. Wagner, 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 -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., Vašák, 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., Vašák, 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., Vašák, 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.
H 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 H 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., Vašák 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 -amylase inhibitor Tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry.
321. Schultze, P., Wörgötter, E., Braun, W., Wagner, G., Vašák, 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 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 -neurotoxin from Dendroaspis polylepis 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.EMBO
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 -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 -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 C 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.
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(,2)-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.