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Biochimica Et Biophysica Acta|March 27, 1979
Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitorA Dubs, G Wagner, K WüthrichEuropean Journal of Biochemistry|September 1, 1978
A 1H nuclear-magnetic-resonance study of the solution conformation of the isoinhibitor K from Helix pomatiaG Wagner, K Wüthrich, H TschescheJournal of Molecular Biology|July 5, 1987
Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonanceG Wagner, D Brühwiler, K WüthrichEuropean Journal of Biochemistry|February 1, 1981
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 structuresG Wagner, A Kumar, K WüthrichEuropean Journal of Biochemistry|December 15, 1983
Protein conformation and proton nuclear-magnetic-resonance chemical shiftsA Pardi, G Wagner, K WüthrichBiochemistry|December 3, 1985
Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperatureH Roder, G Wagner, K WüthrichBiochemistry|December 3, 1985
Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitorH Roder, G Wagner, K WüthrichBiophysics of Structure and Mechanism|August 23, 1976
Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). I. 1H NMR studiesG Wagner, A DeMarco, K WüthrichEuropean Journal of Biochemistry|December 3, 1984
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 proteinC I Stassinopoulou, G Wagner, K WüthrichPageof 201