Publications

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A.D. Gossert and G. Wider.
J. Magn. Reson., 337, 107177 (2022). DOI: 10.1016/j.jmr.2022.107177
Relaxation optimized double acquisition (RODA) as an alternative for virtual decoupling of NMR spectra.
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F. van Drogen, R. Mishra, R. Fabian , M.J. Walczak, S.S. Lee, W. Reiter, B. Hegemann, S. Pelet, I. Dohna , A. Binolfi, Z. Yudina, P. Selenko, G. Wider, G. Ammerer and M. Peter.
J. Cell Biol., 218, 3117-3133 (2019). DOI: 10.1083/jcb.201808161
Mechanical stress impairs pheromone signaling via Pkc1-mediated regulation of the MAPK scaffold Ste5.
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R.G. Brinson, J.P. Marino, F. Delaglio, L.W. Arbogast, R.M. Evans, A. Kearsley, G. Gingras, H. Ghasriani, Y. Aubin, G.K. Pierens, X. Jia, M. Mobli, H.G. Grant, D.W. Keizer, K. Schweimer, J. Ståhle, G. Widmalm, E.R. Zartler, C.W. Lawrence, P.N. Reardon, J.R. Cort, P. Xu, F. Ni, S. Yanaka, K. Kato, S.R. Parnham, D. Tsao, A. Blomgren, T. Rundlöf, N. Trieloff, P. Schmieder, A. Ross, K. Skidmore, K. Chen, D. Keire, D.I. Freedberg, T. Suter-Stahel, G. Wider, G. Ilc, J. Plavec, A. Bradley, D.M. Baldisseri, M.L. Sforça, A.C. de Mattos Zeri, J. Yu Wei, C.M. Szabo, C.A. Amezcua, J.B. Jordan and M. Wikström.
mAbs 11, 94-105 (2019). DOI: 10.1080/19420862.2018.1544454
Enabling adoption of 2D-NMR for the higher order structure assessment of monoclonal antibody therapeutics.
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D. Hofmann, L. Salmon, and G. Wider. J. Am. Chem. Soc. 140, 167-175 (2018). DOI: 10.1021/jacs.7b05050
Activity of Tumor Necrosis Factor α Is Modulated by Dynamic Conformational Rearrangements.
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P. Klukowski, M. J. Walczak, A. Gonczarek, J. Boudet, and G. Wider. Bioinformatics 31, 2981-2988 (2015). DOI: 10.1093/bioinformatics/btv318
Computer Vision – Based Automated Peak Picking Applied to Protein NMR Spectra.
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M. Schubert, M. J. Walczak, Markus Aebi, and G. Wider. Angew. Chemie Int. Ed. 54, 7096-7100 (2015). DOI: 10.1002/anie.201502093
Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation.
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D.R. Perez, M. Leibundgut, and G. Wider. Biochemistry, 54, 2205-2213 (2015). DOI:  10.1021/bi5014563
Interactions of the Acyl Chain with the Saccharomyces cerevisiae Acyl Carrier Protein.
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A. Essig, D. Hofmann, D. Münch, S. Gayathri, M. Künzler, P. T. Kallio, H.-G. Sahl, G. Wider, T. Schneider, and M. Aebi. J.  Biol. Chem., 289, 34953 (2014). DOI:  10.1074/jbc.M114.599878
Copsin, a Novel Peptide-based Fungal Antibiotic Interfering with the Peptidoglycan Synthesis.
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B. Krähenbühl, P. Lukavsky and G. Wider. J. Biomol. NMR 59, 231-240 (2014). DOI: 10.1007/s10858-014-9841-3.
Strategy for automated NMR resonance assignment of RNA: application to 48-nucleotide K10.
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D. Cubrilovic, K. Barylyuk, D. Hofmann, M.J. Walczak, M. Gräber, T. Berg, G. Wider, R. Zenobi. Chem. Sci. 5, 2794-2803 (2014). DOI: 10.1039/C3SC53360C.
Direct monitoring of protein–protein inhibition using nano electrospray ionization mass spectrometry.
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B. Krähenbühl, I. El Bakkali, E. Schmidt, P. Güntert and G. Wider. J. Biomol. NMR 59, 87-93 (2014). DOI 10.1007/s10858-014-9829-z
Automated NMR resonance assignment strategy for RNA via the phosphodiester backbone based on high-dimensional through-bond APSY experiments.
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M.J. Walczak, S. Brighton, F. van Drogen, M. Peter, I. Jelesarov and G. Wider. Angew. Chemie Int. Ed. 53, 1320-1323 (2014).
The RING Domain of the Scaffold Protein Ste5 Adopts Molten Globular Character with a High Thermal and Chemical Stability: A NMR Study.
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M.J. Walczak, C. Puorger, R. Glockshuber and G. Wider. J. Mol. Biol. 426, 542-549 (2014).
Intramolecular donor strand complementation in the E. coli type 1 pilus subunit FimA explains the existence of FimA monomers as off-pathway products of pilus assembly that inhibit host cell apoptosis.
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B. Krähenbühl, J. Boudet and G. Wider. J. Biomol. NMR 56, 149-154 (2013).
4D Experiments Measured with APSY for Automated Backbone Resonance Assignments of Large Proteins.
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B. Krähenbühl and G. Wider. CHIMIA 66, 767-771 (2012).
Automated Projection Spectroscopy (APSY) for the Assignment of NMR Resonances of Biological Macromolecules.
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B. Krähenbühl, D. Hofmann, C. Maris and G. Wider. J. Biomol. NMR 52, 141-150 (2012).
Sugar-to-base correlation in nucleic acids with a 5D APSY-HCNCH or two 3D APSY-HCN experiments.
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S. Hiller and G. Wider. Top. Curr. Chem. 316, 21-48 (2012).
Automated Projection Spectroscopy and Its Applications.
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B. Krähenbühl, S. Hiller, G. Wider. J. Biomol. NMR 51, 313-318 (2011).
4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in protein.
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C. Puorger, M. Vetsch, G. Wider and R. Glockshuber. J. Mol.Biol. 412, 520-535 (2011).
Structure, Folding and Stability of FimA, the Main Structural Subunit of Type 1 Pili from Uropathogenic Escherichia coli Strains
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D. Burschowsky, F. Rudolf, G. Rabut, T. Herrmann, M. Peter and G. Wider. J. Biol. Chem. 285, 1364-1373 (2011).
Structural analysis of the conserved ubiquitin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin.
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D. Perez and G. Wider, Biomol. NMR Assign. 3, 133-136 (2009).
1H, 15N, 13C resonance assignment of the acyl carrier protein subunit of the Saccharomyces cerevisiae fatty acid synthase.
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S. Hiller, G. Wider and K. Wüthrich, J. Biomol. NMR 42, 179-195 (2008).
APSY-NMR with proteins: practical aspects and backbone assignment.
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S. Hiller, R. Joss and G. Wider, J. Am. Chem. Soc. 130, 12073-12079 (2008).
Automated NMR Assignment of Protein Side Chain Resonances Using Automated Projection Spectroscopy (APSY).
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V. Galius, C. Leontiou, T. Richmond and G. Wider, J. Biomol. NMR 40, 175-181 (2008).
Projected [1H,15N]-HMQC-[1H,1H]-NOESY for large molecular systems: application to a 121 kDa protein-DNA complex.
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S. Hiller, G. Wider, L.L. Imbach and K. Wüthrich, Angew. Chemie 120, 992-996 (2008).
Wechselwirkungen der hydrophoben Cluster im entfalteten Membranprotein OmpX in Harnstofflösung.
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S. Hiller, G. Wider, L.L. Imbach and K. Wüthrich, Angew. Chemie (Int. Ed.) 47, 977-981 (2008).
Interactions with hydrophobic clusters in the urea-unfolded membrane protein OmpX.
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J. Haugstetter, M.A. Maurer, T. Blicher, M. Pagac, G. Wider, and L. Ellgaard, J. Biol. Chem.  282, 33859-33867 (2007).
Structure-function analysis of the ER oxireductase TMX3 reveals inter-domain stabilization of the N-terminal redoxactive domain.
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S. Hiller, C. Wasmer, G. Wider, and K. Wüthrich, J. Am. Chem. Soc. 129, 10823-10828 (2007).
Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy.
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R. Wimmer and G. Wider, J. Magn. Reson. 187, 184-192 (2007).
Real-time imaging of the spatial distribution of rf-heating in NMR samples during broadband decoupling.
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C. Fernández and G. Wider, Modern Magnetic Resonance, Part 1: Applications in Chemistry, Biological and Marine Sciences (G.A. Webb (Ed.)), 483-492, Springer (2006).
TROSY NMR for Studies of Large Biological Macromolecules in Solution.
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R. Horst, G. Wider, J. Fiaux, E.B. Bertelsen, A.L. Horwich, and K. Wüthrich, Proc Nat. Acad. Sci USA 103, 15445-15450 (2006).
Proton–proton Overhauser NMR spectroscopy with polypeptide chains in large structures.
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C. Fernández and G. Wider, Advanced Techniques in Biophysics, Springer Series in Biophysics, Vol. 10 (J.L. Arrondo & A. Alonso (Eds.)), 89-128, Springer (2006).
NMR Spectroscopy of Large Biological Macromolecules in Solution.
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L. Dreier and G. Wider, Magn. Reson. Chem. 44, S206-S212 (2006).
Concentration measurements by PULCON using X-filtered or 2D NMR spectra.
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F. Fiorito, S. Hiller,  G. Wider and K. Wüthrich, J. Biomol. NMR 35, 27-37 (2006).
Automated Resonance Assignment of Proteins: 6D APSY-NMR
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G. Wider and L. Dreier, J. Am Chem. Soc. 128, 2571-2576 (2006).
Measuring Protein Concentrations by NMR Spectroscopy.
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K.A. Baker, C. Hilty, W. Peti, A. Prince, P.J. Pfaffinger, G. Wider, K. Wüthrich, and S. Choe, Biochemistry 45, 1663-1672 (2006).
NMR-Derived Dynamic Aspects of N-Type Inactivation of a Kv Channel Suggest a Transient Interaction with the T1 Domain.
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D. Lee, C. Hilty, G. Wider, and K. Wüthrich, J. Magn. Reson. 178, 72-76 (2006).
Effective rotational correlation times of proteins from NMR relaxation interference.
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M. Bienko, C.M. Green, N. Crosetto, F. Rudolf, G. Zapart, B. Coull, P. Kannouche, G. Wider, M. Peter, A.R. Lehmann, K. Hofmann, and I. Dikic, Science 310, 1821-1824 (2005).
Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.
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R. Horst, E.B. Bertelsen, J. Fiaux, G. Wider, A.L. Horwich, and K. Wüthrich, Proc. Nat. Acad. Sci. USA 102, 12748–12753 (2005).
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
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S. Hiller, F. Fiorito, K. Wüthrich and G. Wider, Proc. Nat. Acad. Sci. USA 102, 10876-10881 (2005).
Automated projection spectroscopy (APSY).
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S. Hiller, G. Wider, T. Etezady-Esfarjani, R. Horst and K.Wüthrich,  J. Biomol. NMR 32, 61-70 (2005).
Managing the solvent water polarization to obtain improved NMR spectra of large molecular structures.
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G. Wider, Methods Enzymol. 394, 382-398 (2005).
NMR Techniques Used with Very Large Biological Macromolecules in Solution.
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K. Pervushin, G. Wider, H. Iwai,and K. Wüthrich, Biochemistry 43, 13937-13943 (2004).
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
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H. Iwai, G. Wider, and K. Wüthrich, J. Biomol. NMR 29, 395-398 (2004).
NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups.
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C. Hilty, G. Wider, C. Fernández and K. Wüthrich, ChemBioChem 5, 467-473 (2004).
Membrane protein – lipid interactions in mixed micelles studied by NMR with the use of paramagnetic reagents.
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C. Fernández, C. Hilty, G. Wider, P. Güntert and K. Wüthrich, J. Mol. Biol. 336, 1211-1221 (2004).
NMR structure of the integral membrane protein OmpX.
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K. Wüthrich and G. Wider, Magn. Reson. Chem. 41, S80-S88 (2003).
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.
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G. Wider, Magn. Reson. Chem. 41, S56-S63 (2003).
NMR structures of the micelle-bound polypeptide hormone glucagon.
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S. Hiller, A. Kohl, F. Fiorito, T. Herrmann, G. Wider, J. Tschopp, M.G. Grütter and K. Wüthrich, Structure 11, 1199-1205 (2003).
NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain.
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C. Fernández and G. Wider, Curr. Op. Struct. Biol. 13, 570-580 (2003).
TROSY in NMR studies of the structure and function of large biological macromolecules.
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D. Braun, K. Wüthrich and G. Wider, J. Magn. Reson. 165, 89-94 (2003).
Dissection of heteronuclear NMR experiments for studies of magnetization transfer efficiencies.
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C. Hilty, G. Wider, C. Fernández and K. Wüthrich, J. Biomol. NMR 27, 377-382 (2003).
Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles.
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K. Wüthrich and G. Wider, Encyclopedia of Nuclear Magnetic Resonance (D.M. Grant, R.K. Harris, eds.), Vol. 9, pp. 468-477 (2002).
Transverse relaxation-optimized NMR spectroscopy with biomacromolecular structures in solution.
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C. Fernandez, C. Hilty, G. Wider, and K. Wüthrich, Proc. Nat. Acad. Sci. USA 99, 13533-13537 (2002).
Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.
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C. Hilty, C. Fernandez, G. Wider, and K. Wüthrich, J. Biomol. NMR 23, 289-301 (2002).
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
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G. Wider, IEEE Trans. Appl. Superconduct. 12, 740-745 (2002).
High-Resolution Nuclear Magnetic Resonance Applied to Biophysics and Molecular Biology: Highlights and Challenges.
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G. Wider, BioTechniques 29, 1278-1294 (2000).
Structure Determination of Biological Macromolecules in Solution Using NMR Spectroscopy.
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M. Salzmann, K. Pervushin, G. Wider, H. Senn and K. Wüthrich, J. Am. Chem. Soc. 122, 7543-7548 (2000).
NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments.
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M. Salzmann, A. Ross, M. Czisch, and G. Wider, J. Magn. Reson. 143, 223-228 (2000).
Sensitivity gain by simultaneous acquisition of two coherence pathways: the HNCA+ experiment.
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A. Liu, R. Riek, G. Wider, C. von Schroetter, R. Zahn, and K. Wüthrich, J. Biomol. NMR 16, 127-138 (2000).
NMR experiments for resonance assignments of 13C,15N doubly-labeled flexible polypeptides: application to the human prion protein hPrP(23-230).
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R. Zahn, A. Liu, T. Lührs, R. Riek, Ch. von Schroetter, F. López-García, M. Billeter, L. Calzolai, G. Wider and K. Wüthrich, Proc. Nat. Acad. Sci. USA 97, 145-150 (2000).
NMR solution structure of the human prion protein.
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M. Salzmann, G. Wider, K. Pervushin, and K. Wüthrich, J. Biomol. NMR 15, 181-184 (1999).
Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments.
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G. Wider and K. Wüthrich, Cur. Op. Struct. Biol. 9, 594-601 (1999).
NMR spectroscopy of large molecules and multimolecular assemblies in solution.
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K. Pervushin, G. Wider, R. Riek and K. Wüthrich, Proc. Nat. Acad. Sci. USA 96, 9607-9612 (1999).
The 3D NOESY-[1H,15N,1H]-ZQ-TROSY NMR experiment with diagonal peak suppression.
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R. Riek, B. Precheur, Y. Wang, E. A. Mackay, G. Wider, P. Güntert, A. Liu, J. Kägi, and K. Wüthrich, J. Mol. Biol. 291, 417-428 (1999).
NMR structure of the sea urchin (Strongylocentrotus purpuratus) metallothionein MTA.
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K. Wüthrich, M. Billeter, R. Riek, G. Wider, S. Hornemann and R. Glockshuber, Peptide Science - Present and Future (Y. Shimonishi, ed.), Kluwer, Dordrecht, 330-334 (1998).
Prion protein structure and pathology of transmissible spongiform encephalopathies (TSE).
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M. Salzmann, K. Pervushin, G. Wider, H. Senn and K. Wüthrich, J. Biomol. NMR 14, 85-88 (1999).
[13C]-constant-time [15N,1H]-TROSY-HNCA for the sequential assignments of large proteins.
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R. Riek, G. Wider, K. Pervushin and K. Wüthrich, Proc. Nat. Acad. Sci. USA 96, 4918-4923 (1999).
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
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M. Salzmann, G. Wider, K. Pervushin, H. Senn and K. Wüthrich, J. Am. Chem. Soc. 121, 844-848 (1999).
TROSY-type triple-resonance experiments for sequential assignments of large proteins.
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Wüthrich, K., Riek, R., Wider, G., Garcia, F.L., Liu, A., Zahn, R., Billeter, M., Hornemann, S., and Glockshuber, R. Transfus. Clin. Biol. 6, 31 (1999).
Structural biology of prion proteins.
article

R. Glockshuber, S. Hornemann, R. Riek, M. Billeter, G. Wider, S. Liemann, R. Zahn and K. Wüthrich, Prions: Molecular and Cellular Biology (D.A. Harris, ed.), Horizon Scientific Press, Norfolk England, 1-25 (1999).
Folding and three-dimensional NMR structure of the recombinant cellular prion protein from the mouse.
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M. Salzmann, K. Pervushin, G. Wider, H. Senn and K. Wüthrich, Proc. Nat. Acad. Sci. USA 95, 13585-13590 (1998).
TROSY in triple-resonance experiments ­ new perspectives for sequential NMR assignment of large proteins.
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R. Riek, G. Wider, M. Billeter, S. Hornemann, R. Glockshuber and K. Wüthrich, Proc. Nat. Acad. Sci. USA 95, 11667-11672 (1998) .
Prion protein NMR structure and familial human transmissible spongiform encephalopathies.
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K. Pervushin, G. Wider, and K. Wüthrich, J. Biomol. NMR 12, 345-348 (1998).
Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY.
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R. Glockshuber, S. Hornemann, R. Riek, G. Wider, M. Billeter and K. Wüthrich, in Nato ASI Series A: Life Sciences (D. R . O. Morrison, ed.) vol. 295, 203-216 (1998).
Autonomous folding and three-dimensional structure of the carboxy-terminal domain of the mouse prion protein, PrP(121-231).
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M. Pellecchia, R. Fattorusso and G. Wider, J. Am. Chem. Soc. 120, 6824-6825 (1998).
Determination of the dihedral angle PSI based on J coupling measurements in 15N/13C-labeled proteins.
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K. Pervushin, R. Riek, G. Wider, and K. Wüthrich, J. Am. Chem. Soc. 120, 6394-6400 (1998).
Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in 13C-labeled proteins.
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G. Wider, Progr. NMR Spectrosc. 32, 193-275 (1998).
Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution.
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R. Glockshuber, S. Hornemann, M. Billeter, R. Riek, G. Wider, and K. Wüthrich, FEBS Lett. 426, 291-296 (1998). Erratum in FEBS Lett. 431, 129 (1998)
Prion protein structural features indicate possible relations to signal peptidases.
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A. Sobol, G. Wider, H. Iwai and K. Wüthrich, J. Magn. Reson. 130, 262-271 (1998).
Solvent magnetization artifacts in high field NMR studies of macromolecular hydration.
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K. Pervushin, R. Riek, G. Wider, and K. Wüthrich, Proc. Nat. Acad. Sci. 94, 12366-12371 (1997).
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.
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M. Pellechia, G. Wider, H. Iwai, and K. Wüthrich, J. Biomol. NMR 10, 193-197 (1997).
Arginine side chain assignments in uniformely 15N-labelled proteins using the novel 2D HE(NE)HGHZ experiment.
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R. Riek, S. Hornemann, G. Wider, R. Glockshuber and K. Wüthrich, FEBS Lett. 413, 282-288 (1997).
NMR characterization of the full-length recombinant murine prion protein, mPrP(23­231).
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S. Hornemann, C. Korth, B. Oesch, R. Riek, G. Wider, K. Wüthrich and R. Glockshuber, FEBS Lett. 413, 277-281 (1997).
Recombinant full length murine protein, mPRP(23­231): Purification and spectroscopic characterization.
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R. Glockshuber, S. Hornemann, R. Riek, G. Wider, M. Billeter and K. Wüthrich, Trends Biochem. Sci. 22, 241-242 (1997).
Three-dimensional NMR structure of a self-folding domain of the prion protein, PrP(121-231).
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M. Billeter, R. Riek, G. Wider, S. Hornemann, R. Glockshuber and K. Wüthrich, Proc. Nat. Acad. Sci. USA 94, 7281-­7285 (1997).
Prion protein NMR structure and species barrier for prion diseases.
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K. Pervushin, G. Wider, and K. Wüthrich, J. Am. Chem Soc. 119, 3842-3843 (1997).
Deuterium relaxation in a uniformly 15N labeled homeodomain and its DNA complex.
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O. Schott, M. Billeter, B. Leiting, G. Wider, and K. Wüthrich, J. Mol.Biol. 267, 673-683 (1997).
The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.
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K. Wüthrich, M. Billeter, P. Güntert, P. Luginbühl, R. Riek, and G. Wider, Faraday Disc. 103, 245-253 (1996).
NMR Studies of the Hydration of Biological Macromolecules.
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G. Wider, R. Riek, and K. Wüthrich, J. Am. Chem Soc. 118, 11629-11634 (1996).
Diffusion Filters for Separation of Solvent­Protein and Protein­Protein Nuclear Overhauser Effects (HYDRA).
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E. Kupce, R. Freeman, G. Wider, and K. Wüthrich, J. Magn. Reson. A 122, 81-84 (1996).
Suppression of Cycling Sidebands using Bi-level Adiabatic Decoupling.
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R. Glockshuber, S. Hornemann, R. Riek, M. Billeter, G. Wider and K. Wüthrich, Spektrum der Wissenschaft 9/96, 16-18 (1996).
Dreidimensionale Struktur einer Domäne des zellulären Prion-Proteins aufgeklärt.
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R. Riek, S. Hornemann, G. Wider, M. Billeter, R. Glockshuber and K. Wüthrich, Nature 382, 180-182 (1996).
NMR Structure of the Mouse Prion Protein Domain PrP(121-231).
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E. Kupce, R. Freeman, G. Wider, and K. Wüthrich, J. Magn. Reson. A 120, 264-268 (1996).
Figure of Merit and Cycling Sidebands in Adiabatic Decoupling Schemes.
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D. Braun, G. Wider, and K. Wüthrich, J. Magn. Reson. B 110, 313-315 (1996).
Monitoring NMR Spectrometer Performance during Data Accumulation for Macromolecular Structure Determination.
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V. Dötsch, G. Wider, G. Siegal, and K. Wüthrich, FEBS Lett. 372, 288-290 (1995).
Salt-stabilized Globular Protein Structure in 7 M Aqueous Urea Solution.
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V. Dötsch, G. Wider, G. Siegal, and K. Wüthrich, FEBS Lett. 366, 6-10 (1995).
Interaction of Urea with an Unfolded Protein. The DNA-binding Domain of the 434-Repressor.
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V. Dötsch and G. Wider, J. Am. Chem. Soc. 117, 6064-6070 (1995).
Exchange Rates of Internal Water Molecules in Proteins Measured Using Pulsed Field Gradients.
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D. Braun, G. Wider, and K. Wüthrich, J. Am. Chem. Soc. 116, 8466-8469 (1994).
Sequence-Corrected 15N "Random Coil" Chemical Shifts.
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V. Dötsch, G. Wider, and K. Wüthrich, J. Magn. Reson. 109A, 263-264 (1994).
Phase-Sensitive Spectra in a Single Scan with Coherence Selection by Pulsed Field Gradients.
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C. Spitzfaden, W. Braun, G. Wider, H. Widmer and K. Wüthrich, J. Biomol. NMR 4, 463-482 (1994).
Determination of the NMR solution structure of the cyclophilin A - cyclosporin A complex.
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G. Wider, V. Dötsch, and K. Wüthrich, J. Magn. Reson. 108A, 255-258 (1994).
Self-Compensating Pulsed Magnetic-Field Gradients for Short Recovery Times.
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T. Szyperski, G. Wider, J. Bushweller, and K. Wüthrich, J. Am. Chem Soc. 115, 9307 -9308 (1993).
Reduced Dimensionality in Triple-Resonance NMR Experiments.
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G. Wider and K. Wüthrich, J. Magn. Reson. 102B, 239-241 (1993).
A Simple Experimental Scheme Using Pulsed Field Gradients for Coherence-Pathway Rejection and Solvent Suppression in Phase-Sensitive Heteronuclear Correlation Spectra.
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T. Szyperski, G. Wider, J. Bushweller, and K. Wüthrich, J. Biomol. NMR. 3, 127-132 (1993).
3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins.
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P. Güntert, V. Dötsch, G. Wider, and K. Wüthrich, J. Biomol. NMR 2, 619-629 (1992).
Processing of Multi-Dimensional NMR Data with the New Software PROSA.
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D. Neri, M. Billeter, G. Wider, and K. Wüthrich, Science 257, 1559-1563 (1992).
NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
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D. Neri, G. Wider, and K. Wüthrich, FEBS Lett. 303, 129-135 (1992).
1H, 15N, 13C NMR Assignments of the 434 Repressor Fragments 1-63 and 44-63 Unfolded in Urea.
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J. Vendrell, A. Guasch, M. Coll, V. Villegas, M. Billeter, G. Wider, R. Huber, K. Wüthrich, and F. Aviles, Biol. Chem. Hoppe-Seyler 373, 387-392 (1992).
Pancreatic Procarboxypeptidases: Their Activation Processes Related to the Structural Features of the Zymogens and Activation Segments.
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C. Spitzfaden, H.-P. Weber, W. Braun, J. Kallen, G. Wider, H. Widmer, M. Walkinshaw, and K. Wüthrich, FEBS Lett. 300, 291-300 (1992).
Cyclosporin A - Cyclophilin: A Model based on X-ray and NMR Data.
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D. Neri, G. Wider, and K. Wüthrich, Proc. Natl. Acad. Sci. (USA) 89, 4397-4401 (1992).
Complete 15N and 1H NMR Assignments for the Amino-Terminal Domain of the 434 Repressor in the Urea-Unfolded Form.
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M. Billeter, J. Vendrell, G. Wider, F. Aviles, M. Coll, A. Guasch, R. Huber and K. Wüthrich, J. Biomol. NMR 2, 1-10 (1992).
Comparison of the NMR Solution Structure with the X-ray Crystal Structure of the Activation Domain from Procarboxypeptidase B.
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K. Wüthrich, B. von Freyberg, C. Weber, G. Wider, R. Traber, H. Widmer, and W. Braun, Science 254, 953-954 (1991).
Receptor-Induced Conformation Change of the Immunosuppressant Cyclosporin A.
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J. Kallen, C. Spitzfaden, M. Zurini, G. Wider, H. Widmer, K. Wüthrich, and M. Walkinshaw, Nature 353, 276-279 (1991).
Structure of Human Cyclophilin and its Binding Site for Cyclosporin A Determined by X-ray Crystallography and NMR Spectroscopy.
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K. Wüthrich, C. Spitzfaden, K. Memmert, H. Widmer, and G. Wider, FEBS Lett. 285, 237-247 (1991).
Protein Secondary Structure Determination by NMR - Application with Recombinant Cyclophilin.
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G. Wider, D. Neri, and K. Wüthrich, J. Biomol. NMR 1, 93 - 98 (1991).
Studies of Slow Conformational Equilibria in Macromolecules by Exchange of Heteronuclear Longitudinal 2-Spin-Order in a 2D Difference Correlation Experiment.
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G. Wider, C. Weber, and K. Wüthrich, J. Am. Chem. Soc. 113, 4676-4678 (1991).
Proton-Proton Overhauser Effects of Receptor-Bound Cyclosporin A Observed with the Use of a Heteronuclear-Resolved Half-Filter Experiment.
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C. Weber, G. Wider, B. von Freyberg, R. Traber, W. Braun, H. Widmer, and K. Wüthrich, Biochemistry 30, 6563-6574 (1991).
The NMR Structure of Cyclosporin A bound to Cyclophilin in Aqueous Solution.
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G. Wider and K. Wüthrich, CHEMTRACTS 1, 517-519 (1991).
Sequential NMR Assignments of 1H, 13C and 15N Resonances of Large Proteins by Heteronuclear Triple-Resonance 3D NMR Spectroscopy: Application to Calmodulin.
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J. Vendrell, M. Billeter, G. Wider, F.X. Aviles, and K. Wüthrich, EMBO J. 10, 11-15 (1991).
The NMR Structure of the Activation Domain Isolated from Porcine Procarboxypeptidase-B.
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G. Wider, C. Weber, H. Widmer, R. Traber and K. Wüthrich, J. Am. Chem. Soc. 112, 9015-9016 (1990).
Use of a Double-Half-Filter in Two-Dimensional 1H NMR Studies of Receptor-Bound Cyclosporin.
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G. Wider, J. Magn. Reson. 89, 406-409 (1990).
Elimination of Baseline Artifacts in NMR Spectra by Oversampling.
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J. Vendrell, G. Wider, F. X. Aviles and K. Wüthrich, Biochemistry 29, 7515-7522 (1990).
Sequence-Specific Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B.
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K. Wüthrich and G. Wider, CHEMTRACTS 1, 106-108 (1990).
Staphylococcal Nuclease: Sequential Assignments and Solution Structure.
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B.A. Messerle, G. Wider, G. Otting, C. Weber, and K. Wüthrich, J. Magn. Reson. 85, 608-613 (1989).
Solvent Suppression Using a Spin Lock in 2D and 3D NMR Spectroscopy with H2O Solutions.
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G. Wider, D. Neri, G. Otting and K. Wüthrich, J. Magn. Reson. 85, 426-431 (1989).
A Heteronuclear Three-Dimensional NMR Experiment for Measurements of Small Heteronuclear Coupling Constants in Biological Macromolecules.
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D. Neuhaus, G. Wider, G. Wagner and K. Wüthrich, J. Magn. Reson. 57, 164-168 (1984).
X-Relayed 1H-1H Correlated Spectroscopy.
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G. Wider, S. Macura, Anil Kumar, R.R. Ernst and K. Wüthrich, J. Magn. Reson. 56, 207-234 (1984).
Homonuclear Two-Dimensional 1H NMR of Proteins. Experimental Procedures.
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W. Braun, G. Wider, K.H. Lee and K. Wüthrich, J. Mol. Biol. 169, 921-948 (1983).
Conformation of Glucagon in a Lipid-Water Interphase by 1H Nuclear Magnetic Resonance.
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A. Pardi, R. Walker, H. Rapoport, G. Wider and K. Wüthrich, J. Am. Chem. Soc. 105, 1652-1653 (1983).
Sequential Assignments for the 1H and 31P Atoms in the Backbone of Oligonucleotides by Two-Dimensional Nuclear Magnetic Resonance.
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P. Strop, G. Wider and K. Wüthrich, J. Mol. Biol. 166, 641-667 (1983).
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.
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G. Wider, R.V. Hosur and K. Wüthrich, J. Magn. Reson. 52, 130-135 (1983).
Suppression of the Solvent Resonance in 2D NMR Spectra of Proteins in H2O Solution.
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R.V. Hosur, G. Wider and K. Wüthrich, Eur. J. Biochem. 130, 497-508 (1983).
Sequential Individual Resonance Assignments in the 1H Nuclear Magnetic Resonance Spectrum of Cardiotoxin VII2 from Naja mossambica mossambica.
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K. Wüthrich, C. Bösch, W. Braun, L.R. Brown, K.H. Lee and G. Wider, in "Structure of Complexes between Biopolymers and Low Molecular Weight Molecules", Workshop Conference Hoechst, Vol. 11, eds. W. Bartmann & G. Snatzke, J. Wiley, New York, p. 145-156, 1982. NMR Studies of the Conformation of Polypeptide Chains Bound to Lipid Micelles.
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A.S. Arseniev, G. Wider, F.J. Joubert and K. Wüthrich, J. Mol. Biol. 159, 323-351 (1982).
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.
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G. Wider, Dissertation ETH Nr. 7040, Zürich, Switzerland (1982).
Zweidimensionale Kernresonanz-Spektroskopie von Polypeptiden und Proteinen. Anwendung für Konformationsstudien von an volldeuterierte Lipid-Micellen gebundenem Glucagon.
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R.V. Hosur, G. Wider and K. Wüthrich, Experientia 38, 726 (1982).
Spatial Structures of Snake Venom Toxins by NMR: Sequential 1H NMR Assignments in Cardiotoxin VII2 from Naja mossambica mossambica.
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G. Wider, K.H. Lee and K. Wüthrich, J. Mol. Biol. 155, 367-388 (1982).
Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra: Glucagon Bound to Perdeuterated Dodecylphosphocholine Micelles.
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K. Wüthrich, G. Wider, G. Wagner and W. Braun, J. Mol. Biol. 155, 311-319 (1982).
Sequential Resonance Assignments as a Basis for Determination of Spatial Protein Structures by High Resolution Proton Nuclear Magnetic Resonance.
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R. Baumann, G. Wider, R.R. Ernst and K. Wüthrich, J. Magn. Reson. 44, 402-406 (1981).
Improvement of 2D NOE and 2D Correlated Spectra by Symmetrization.
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G. Wider, R. Baumann, K. Nagayama, R.R. Ernst and K. Wüthrich, J. Magn. Reson. 42, 73-87 (1981).
Strong Spin-Spin Coupling in the Two-Dimensional J-Resolved 360 MHz 1H NMR Spectra of the Common Amino Acids.
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R. Schwyzer, V.M. Kriwaczek, K. Baumann, H.-R. Haller, G. Wider and P. Wiltzius, Pure and Appl. Chem. 51, 831-835 (1979).
Hormone-Receptor Interactions: A Study of the Binding of Hormone-Substituted Tobacco Mosaic Virus to Membrane Vesicles by Dynamic Light Scattering and by Electric Birefrigence.
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