References 1990 - 1999

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., Vašák, 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 and 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 ³J_HN in proteins.

361. Leupin, W., Otting, G., Amacker, H. and Wüthrich, K. (1990) FEBS Lett. 263, 313–316.
Application of ¹³C(_l )-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, 825–831.
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, 9015–9016.
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) Japanese Edition of 'NMR of Proteins and Nucleic Acids' (translation by Y. Kyogoku and Y. Kobayashi). 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 H_NNH_AB-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 and 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.
FLATTA 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 phage434 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 ³J_HN 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., Vašák, 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 (C14S) 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 -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., Vašák, 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. Qian, 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–.
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 and 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.

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 -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 and 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 -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.

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.

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 H^/C^/(CO)NHN, a projected 4D NMR experiment for sequential correlation of polypeptide ¹H^/, ¹³C^/ and backbone ¹⁵N and ¹H^N 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 2, 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 Proc. 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, World Scientific, Singapore.

487. Szyperski, 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. Biomol. 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 urea solution.

490. Brunne, R.M., Berndt, K.D., Güntert, P., Wüthrich, K. and van Gunsteren, W.F. (1995) Proteins 23, 49–62.
Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations.

491. Luginbühl, P., Szyperski, T. and Wüthrich, K. (1995) J. Magn. Reson. B 109, 229–233.
Statistical basis for the use of ¹³C^ chemical shifts in protein structure determination.

492. Schiffer, C.A., Dötsch, V., Wüthrich, K. and van Gunsteren, W. (1995) Biochemistry 34, 15057–15067.
Exploring the role of the solvent in the denaturation of a protein: A molecular dynamics study of the DNA binding domain of the 434 repressor.

493. Altmann, S., Labhardt, A.M., Bur, D., Lehmann, C., Bannwarth, W., Billeter, M., Wüthrich, K. and Leupin, W. (1995) Nucl. Acids Res., 23, 4827–4835.
NMR studies of DNA duplexes singly cross-linked by different synthetic linkers.

494. Bartels, C., Güntert, P. and Wüthrich, K. (1995) J. Magn. Reson. A 117, 330–333.
IFLAT – A new automatic baseline-correction method for multidimensional NMR spectra with strong solvent signals.

495. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 1, pp. 710–719.
NMR structures of biological macromolecules.

496. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 2, pp. 932–939.
Biological macromolecules: structure determination in solution.

497. Wüthrich, K. (1996) in Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant and R.K. Harris, eds.) Wiley, New York, Vol. 5, pp. 3449–3455.
Pancreatic trypsin inhibitor.

498. Berndt, K.D., Güntert, P. and Wüthrich, K. (1996) Proteins 3, 304–313.
Conformational sampling by NMR solution structures calculated with the program DIANA evaluated by comparison with long-time molecular dynamics calculations in explicit water.

499. Koradi, R, Billeter, M. and Wüthrich, K (1996) J. Mol. Graph. 14, 51–55.
MOLMOL: a program for display and analysis of macromolecular structures.

500. Zerbe, O., Szyperski, T., Ottiger, M. and Wüthrich, K. (1996) J. Biomol. NMR 7, 99–106.
Three-dimensional ¹H-TOCSY-relayed ct-[¹³C,¹H]-HMQC for aromatic spin system identification in uniformly ¹³C labeled proteins.

501. Braun, D., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. B 110, 313–315.
Monitoring NMR spectrometer performance during data accumulation for macromolecular structure determination.

502. Bartels, C., Billeter, M., Güntert, P. and Wüthrich, K. (1996) J. Biomol. NMR 7, 207–213.
Automated sequence-specific NMR assignment of homologous proteins using the program GARANT.

503. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wüthrich, K. (1996) Nature 382, 180–182.
NMR structure of the mouse prion protein domain PrP(121–231).

504. Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C. and Wüthrich, K. (1996) J. Mol. Biol. 260, 236–250.
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.

505. Billeter, M., Güntert, P., Luginbühl, P. and Wüthrich, K. (1996) Cell 85, 1057–1065.
Hydration and DNA recognition by homeodomains.

506. Kupce, E., Freeman, R., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. A 120, 264– 268.
Figure of merit and cycling sidebands in adiabatic decoupling.

507. Antuch, W., Güntert, P. and Wüthrich, K. (1996) Nature Struct. Biol. 3, 662–665.
Ancestral -crystallin percursor structure in a yeast killer toxin.

508. Luginbühl, P., Wu, J., Zerbe, O., Ortenzi, C., Luporini, P. and Wüthrich, K. (1996) Protein Science 5, 1512–1522.
The NMR solution structure of the pheromone Er-11 from the cilitated protozoan Euplotes raikovi.

509. Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G. and Wüthrich, K. (1996) Spektrum der Wissenschaften 9, 16–18.
Dreidimensionale Struktur einer Domäne des zellulären Prion-Proteins aufgeklärt.

510. Szypersky, T., Bailey, J.E. and Wüthrich, K. (1996) Trends Biotechn. 14, 453–459.
Detecting and dissecting metabolic fluxes using biosynthetic fractional ¹³C-labeling and two-dimensional NMR spectroscopy.

511. Szyperski, T., Braun, D., Banecki, B. and Wüthrich, K. (1996) J. Am. Chem. Soc. 118, 8146–8147.
Useful information from axial peak magnetization in projected NMR experiments.

512. Wüthrich, K. (1996) in Molecular Manufacturing, EL.B.A. Forum Series, Vol. 2 (C. Nicolini and S. Vakula, eds.) pp. 115–130, Plenum Press, New York.
NMR structure determination and rational drug design.

513. Kupce, E., Freeman, R., Wider, G. and Wüthrich, K. (1996) J. Magn. Reson. A 122, 81–84.
Suppression of cycling sidebands using bi-level adiabatic decoupling.

514. Luginbühl, P., Güntert, P., Billeter, M. and Wüthrich, K. (1996) J. Biomol. NMR 8, 136– 146.
The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.

515. Wider, G., Riek R. and Wüthrich, K. (1996) J. Am. Chem. Soc. 118, 11629–11634.
Diffusion filters for separation of solvent–protein and protein–protein nuclear Overhauser effects (HYDRA).

516. Pervushin, K., Billeter, M., Siegal, G. and Wüthrich, K. (1996) J. Mol. Biol. 264, 1002– 1012.
Structural role of a buried salt bridge in the 434 repressor DNA-binding domain.

517. Bartels, C., Güntert, P., Billeter, M. and Wüthrich, K. (1997) J. Comp. Chem. 18, 139–149.
GARANT– a general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra.

518. Pellecchia, M., Iwai, H., Szyperski, T. and Wüthrich, K. (1997) J. Magn. Reson. 124, 274– 278.
The 2D NMR experiments H(C)CO₂ and HCCO₂ for assignment and pH titration of carboxylate groups in uniformly ¹⁵N/¹³C-labeled proteins.

519. Wüthrich, K. (1997) Chimia 51, 16–17.
Structural insight into prion diseases.

520. Fernández ,C., Szyperski, T., Bruyère, T., Ramage, P., Mösinger, E. and Wüthrich, K. (1997) J. Mol. Biol. 266, 576–593.
NMR solution structure of the pathogenesis-related protein P14a.

521. Wüthrich, K., Billeter, M., Güntert, P., Luginbühl, P., Riek, R. and Wider, G. (1996) Faraday Discuss. 103, 245–253.
NMR studies of the hydration of biological macromolecules.

522. Schott, O., Billeter, M., Leiting, B., Wider, G. and Wüthrich, K. (1997) J. Mol. Biol. 267, 673–683.
The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.

523. Sauer, U., Hatzimanikatis, V., Bailey, J.E., Hochuli, M., Szyperski, T. and Wüthrich, K. (1997) Nature Biotech. 15, 448–452.
Metabolic fluxes in riboflavin-producing Bacillus subtilis.

524. Pervushin, K., Wider, G. and Wüthrich, K. (1997) J. Am. Chem. Soc. 119, 3842– 3843.
Deuterium relaxation in a uniformly ¹⁵N-labeled homeodomain and its DNA complex.

525. Luginbühl, P., Pervushin, K.V., Iwai, H. and Wüthrich, K. (1997) Biochemistry 36, 7305–7312.
Anisotropic molecular rotational diffusion in ¹⁵N spin relaxation studies of protein mobility.

526. Wüthrich, K. (1996) Proc. Natl. Acad. Sci. India 66, 1–8.
NMR for physicochemical characterization of proteins.

527. Wüthrich, K. (1997) in Röntgen Centennial: X-rays in Natural and Life Sciences (A. Haase, G. Landwehr and E. Umbach, eds.) pp. 242–257, World Scientific, Singapore.
NMR - an alternative to x-ray crystallography for protein and nucleic acid structure determination.

528. King, C.Y., Trittmann, P., Gross, H., Gebert, R., Aebi, M. and Wüthrich, K. (1997) Proc. Natl. Acad Sci. USA 94, 6618–6622.
Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments.

529. Billeter, M., Riek, R., Wider, G., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA 94, 7281–7285.
Prion protein NMR structure and species barrier for prion diseases.

530. Glockshuber, R., Hornemann S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1997) Trends Biochem. Sci. 22, 241–242.
Three-dimensional NMR structure of a self-folding domain of the prion protein PrP(121–231).

531. Altmann, S., Labhardt, A.M., Senn, H. and Wüthrich, K. (1997) J. Biomol. NMR 9, 445–446.
Sequence-specific 1H, 13C and 15N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH.

532. Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wüthrich, K. and Glockshuber, R. (1997) FEBS Lett. 413, 277–281.
Recombinant full-length murine prion protein, mPrP(23–231): purification and spectroscopic characterization.

533. Riek, R., Hornemann, S., Wider, G., Glockshuber, R. and Wüthrich, K. (1997) FEBS Lett. 413, 282–288.
NMR characterization of the full length recombinant murine prion protein, mPrP(23–231).

534. Nieba-Axmann, S. E., Ottiger, M., Wüthrich, K. and Plückthun, A. (1997) J. Mol. Biol. 271, 803–818.
Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.

535. Ottiger, M., Zerbe, O., Güntert, P. and Wüthrich, K. (1997) J. Mol. Biol. 272, 64–81.
The NMR solution conformation of unligated human cyclophilin A.

536. Güntert, P., Mumenthaler, C. and Wüthrich, K. (1997) J. Mol. Biol. 273, 283–298.
Torsion angle dynamics for NMR structure calculation with the new program DYANA.

537. Pellecchia, M., Wider, G., Iwai, H. and Wüthrich, K. (1997) J. Biomol. NMR 10, 193–197.
Arginine side chain assignments in uniformly ¹⁵N-labeled proteins using the novel 2D HE(NE)HGHH experiment.

538. Klimasauskas, S., Szyperski, T., Serva, S. and Wüthrich, K. (1998) EMBO J. 17, 317–324.
Dynamic modes of the flipped-out cytosine during HhaI methyltransferase–DNA interactions in solution.

539. Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1997) Proc. Natl. Acad. Sci. USA 94, 12366–12371.
Attenuated T₂ relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution.

540. Korth, C., Stierli, E., Streit, P., Moser, M., Schaller, O., Fischer, R., Schulz-Schaeffer, W., Kretschmar, H., Raeber, A., Braun, U., Ehrensperger, F., Hornemann, S., Glockshuber, R., Riek, R., Billeter, M., Wüthrich, K. and Oesch, B. (1997) Nature 390, 74–77.
Prion (PrP^Sc)-specific epitope defined by a monoclonal antibody.

541. Szyperski, T., Ono A., Fernández C., Iwai H., Tate, S., Wüthrich, K. and Kainosho, M. (1997) J. Am. Chem. Soc. 119, 9901–9902.
Measurement of ³J_C2’P scalar couplings in a 17 kDa protein complex with ¹³C,¹⁵N-labeled DNA distinguishes the B_I and B_II phosphate conformations of the DNA.

542. Zahn, R., von Schroetter C. and Wüthrich, K. (1997) FEBS Lett. 417, 400–404.
Human prion proteins expressed in Echerichia coli and purified by high-affinity column refolding.

543. Szyperski, T., Férnandez C. and Wüthrich K. (1997) J. Magn. Reson. 128, 228–232.
Two-Dimensional ct-HC(C)H-COSY for resonance assignments of smaller ¹³C-labeled biomolecules.

544. Mumenthaler, C., Güntert, P., Braun, W. and Wüthrich, K. (1997) J. Biomol. NMR 10, 351– 362.
Automated combined assignment of NOESY spectra and three-dimensional protein structure determination.

545. Glockshuber, R., Hornemann, S., Billeter, M., Riek, R., Wider, G., and Wüthrich, K. (1998) FEBS Lett. 426, 291–296.
Prion protein structural features indicate possible relations to signal peptidases.

546. Szyperski, T., Férnandez, C., Ono, A., Kainosho, M. and Wüthrich, K. (1998) J. Am. Chem. Soc. 120, 821–822.
Measurement of deoxyribose ³J_HH scalar couplings reveals protein binding-induced changes in the sugar puckers of the DNA.

547. Szyperski, T., Férnandez, C., Mumenthaler, C. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 2262–2266.
Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system.

548. Sobol, A. G., Wider, G., Iwai, H. and Wüthrich, K. (1998) J. Magn. Reson. 130, 262–271.
Solvent magnetization artifacts in high-field NMR studies of macromolecular hydration.

549. Pellecchia, M., Güntert, P., Glockshuber, R. and Wüthrich, K. (1998) J. Biomol. NMR 11, 229–230.
Sequence-specific ¹H, ¹⁵N and ¹³C assignments of the periplasmic chaperone FimC from Escherichia coli.

550. Pervushin, K., Riek, R., Wider, G. and Wüthrich, K. (1998) J. Am. Chem. Soc. 120, 6394– 6400.
Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in ¹³C-labeled proteins.

551. Wüthrich, K. (1998) Nature Struct. Biol. 5, 492–495.
The second decade – into the third millenium.

552. Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes. B. D., Wright, P. E. and Wüthrich, K. (1998) Pure Appl. Chem. 70, 117–142; reprinted: (1998) J. Biomol NMR, 12, 1–23; (1998) J. Mol. Biol. 280, 933–952.
Recommendations for the presentation of NMR structures of proteins and nucleic acids.

553. Glockshuber, R., Hornemann, S., Riek, R., Wider, G., Billeter, M. and Wüthrich, K. (1998) in NATO ASI Series A: Life Sciences (D. R. O. Morrison, ed.) vol. 295, pp. 203–216.
Autonomous folding and three-dimensional structure of the carboxy-terminal domain of the mouse prion protein, PrP(121–231).

554. Weber, F. E., Dyer, J. H., Lopez Garcia, F., Werder, M., Szyperski, T., Wüthrich, K. and Hauser, H. (1998) Cell. Mol. Life Sci. 54, 751–759.
In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1–20 is flexibly disordered, and residues 21–143 adopt the same globular fold as in mature SCP2.

555. Pervushin, K. V., Wider, G. and Wüthrich, K. (1998) J. Biomol. NMR 12, 345–348.
Single transition-to-single transition polarization transfer (ST2-PT) in [¹⁵N,¹H]-TROSY.

556. Fernàndez C., Szyperski, T., Ono, A., Iwai, H., Tate, S., Kainosho, M. and Wüthrich, K. (1998) J. Biomol. NMR 12, 25–37.
NMR with ¹³C,¹⁵N-doubly-labeled DNA: The Antennapedia homeodomain complex with a 14-mer DNA duplex.

557. Pellecchia, M., Güntert, P., Glockshuber R. and Wüthrich, K. (1998) Nature Struct. Biol. 5, 10, 885–890.
NMR solution structure of the periplasmic chaperone FimC.

558. Riek, R., Wider, G., Billeter, M., Hornemann, S., Glockshuber R. and Wüthrich K. (1998) Proc. Natl. Acad. Sci. USA 95, 11667–11672.
Prion protein NMR structure and familial human spongiform encephalopathies.

559. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 13585–13590
TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins.

560. Banci, L., Bertini, I., Cremonini, M.A., Gori-Savellini, G., Luchinat, C., Wüthrich, K. and Güntert, P. (1998) J. Biomol. NMR 12, 553–557.
PSEUDYANA for NMR structure calculation of paramagnetic metalloproteins using torsion angle molecular dynamics.

561. Güntert, P., Billeter, M., Ohlenschläger, O., Brown, L.R. and Wüthrich, K. (1998) J. Biomol. NMR 12, 543–548.
Conformational analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND.

562. Glockshuber, R., Hornemann, S., Riek, R., Billeter, M., Wider, G., Liemann, S., Zahn, R. and Wüthrich, K. (1998) in PRIONS - Molecular and Cellular Biology (D. A. Harris, ed.) Horizon Scientific Press, pp. 1–25.
Folding and three-dimensional NMR structure of the recombinant cellular prion protein from the mouse.

563. Pervushin, K., Ono, A., Fernandez, C., Szyperski, T., Kainosho, M. and Wüthrich, K. (1998) Proc. Natl. Acad. Sci. USA 95, 14147–14151.
NMR scalar couplings across Watson–Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.

564. Koradi, R., Billeter, M., Engeli, M., Güntert, P., and Wüthrich, K. (1998) J. Magn. Reson. 135, 288–297.
Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY.

565. Szyperski, T., Vandenbussche, G., Curstedt, T., Ruysschaert, J.-M., Wüthrich, K. and Johansson J. (1998) Protein Science 7, 2533–2540.
Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric -helical state into insoluble -sheet aggregates.

566. Salzmann, M., Wider, G., Pervushin, K., Senn, H. and Wüthrich, K. (1999) J. Am. Chem. Soc. 121, 844–848.
TROSY-type triple resonance experiments for sequential NMR assignments of large proteins.

567. Fiaux, J., Andersson, Ch.I.J., Holmberg, N., Bülow, L., Kallio, P.T., Szypersky, T., Bailey, J.E. and Wüthrich, K. (1999) J. Am. Chem. Soc. 121, 1407–1408.
¹³C NMR flux ratio analysis of Escherichia coli central carbon metabolism in microaerobic bioprocesses.

568. Pellecchia, M., Sebbel, P., Hermanns, U., Wüthrich, K. and Glockshuber, R. (1999) Nature Struct. Biol. 6, 336–339.
Pilus chaperone FimC–adhesin FimH interactions mapped by TROSY-NMR.

569. Fattorusso, R., Pellecchia, M., Viti, F., Neri. P., Neri, D. and Wüthrich, K. (1999) Structure with Folding and Design 7, 381–390.
NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis.

570. Szyperski, T., Götte, M., Billeter, M., Perola, E., Cellai, L., Heumann, H. and Wüthrich, K. (1999) J. Biomol. NMR 13, 343–355.
NMR structure of the chimeric hybrid duplex r(gcaguggc)•r(gcca)d(CTGC) comprising the tRNA-DNA junction formed during initiation of HIV-1 reverse transcription.

571. Riek, R., Wider, G., Pervushin, K. and Wüthrich, K. (1999) Proc. Natl. Acad. Sci. USA 96, 4918–4923.
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.

572. Hochuli, M., Patzelt, H., Oesterhelt, D., Wüthrich, K. and Szyperski, T. (1999) J. Bacteriol. 181, 3226–3237.
Amino acid biosynthesis in the halophilic archaeon Haloarcula hispanica.

573. Matthey, U., Kaim, G., Braun, D., Wüthrich, K. and Dimroth, P. (1999) Eur. J. Biochem. 261, 459–467.
NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles.

574. Salzmann, M., Pervushin, K., Wider, G., Senn, H. and Wüthrich, K. (1999) J. Biomol. NMR 14, 85–88.
[¹³C]-constant-time [¹⁵N,¹H]-TROSY-HNCA for sequential assignments of large proteins.

575. Wüthrich, K., Billeter, M., Riek, R., Wider, G., Hornemann, S. and Glockshuber, R. (1999) in Peptide Science - Present and Future (Y. Shimonishi, ed.) pp. 330–334, Kluwer, Dordrecht.
Prion protein structure and pathology of transmissible spongiform encephalopathies (TSE).

576. Liu, A., Riek, R., Zahn, R., Hornemann, S., Glockshuber, R. and Wüthrich, K. (1999) Biopolymers Peptide Sci. 51, 145–152.
Peptides and proteins in neurodegenerative disease: helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy.

577. Wimmer, R., Herrmann, T., Solioz, M. and Wüthrich, K. (1999) J. Biol. Chem. 274, 22597–22603.
NMR structure and metal interactions of the CopZ copper chaperone.

578. Pervushin, K.V., Wider, G., Riek, R. and Wüthrich, K. (1999) Proc. Natl. Acad. Sci. USA 96, 9607–9612.
The 3D NOESY-[¹H,¹⁵N,¹H]-ZQ-TROSY NMR experiment with diagonal peak suppression.

579. Riek, R., Prêcheur, B., Wang, Y., Mackay, E.A., Wider, G., Güntert, P., Liu, A., Kägi J.H.R. and Wüthrich, K. (1999) J. Mol. Biol. 291, 417–428.
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.

580. Fernàndez, C., Szyperski, T., Billeter, M., Ono, A., Iwai, H., Kainosho, M. and Wüthrich, K. (1999) J. Mol. Biol. 292, 609–617.
Conformational changes of the BS2 operator DNA upon complex formation with the Antennapedia homeodomain studied by NMR with ¹³C/¹⁵N-labeled DNA.

581. Wider, G. und Wüthrich, K. (1999) Curr. Opin. Struct. Biol. 9, 594–601.
NMR spectroscopy of large molecules and multimolecular assemblies in solution.

582. Wüthrich, K. (1999) in Biological Physics, AIP Conf. Proc. 487, 3–7.
Hydration of proteins, nucleic acids and protein–DNA complexes in solution.

583. Szyperski, T., Fernandéz, C., Ono, A., Wüthrich, K. and Kainosho, M. (1999) J. Magn. Reson. 140, 491–494.
The 2D {³¹P} spin-echo-difference constant-time [¹³C,¹H]-HMQC experiment for simultaneous determination of ³J_H3’P and ³J_C4’P in ¹³C-labeled nucleic acids and their protein complexes.

584. Szyperski, T., Glaser, R.W., Hochuli, M., Fiaux, J., Sauer, U., Bailey, J.E. and Wüthrich, K. (1999) Metabolic Eng. 1, 189–197.
Bioreaction network topology and metabolic flux ratio analysis by biosynthetic fractional ¹³C labeling and two-dimensional NMR spectroscopy.

585. Sauer, U., Lasko, D.R., Fiaux, J., Hochuli, M., Glaser, R., Szyperski, T., Wüthrich, K. and Bailey, J.E. (1999) J. Bacteriol. 181, 6679–6688.
Metabolic Flux Ratio (METAFoR) analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism.

586. Salzmann, M., Wider, G., Pervushin, K. and Wüthrich, K. (1999) J. Biomol. NMR 15, 181– 184.
Improved sensitivity and coherence selection for [¹⁵N,¹H]-TROSY elements in triple resonance experiments.

587. Wüthrich, K. (1999) in Hydration Processes in Biology (M.C. Bellissent-Funel, ed.) pp. 251–258, IOS Press, Amsterdam.
NMR structure determination of biological macromolecules and studies of hydration in solution.