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Results: 1-8 |
Results: 8
Rational design and molecular characterization of a chimaeric response regulator protein
Authors: Bock, A Bantscheff, M Perraud, AL Rippe, K Weiss, V Glocker, MO Gross, R
Citation: A. Bock et al., Rational design and molecular characterization of a chimaeric response regulator protein, J MOL BIOL, 310(2), 2001, pp. 283-290
Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone
Authors: Barbirz, S Jakob, U Glocker, MO
Citation: S. Barbirz et al., Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone, J BIOL CHEM, 275(25), 2000, pp. 18759-18766
Multiple and subsequent MALDI-MS on-target chemical reactions for the characterization of disulfide bonds and primary structures of proteins
Authors: Happersberger, HP Bantscheff, M Barbirz, S Glocker, MO
Citation: Hp. Happersberger et al., Multiple and subsequent MALDI-MS on-target chemical reactions for the characterization of disulfide bonds and primary structures of proteins, METH MOL B, 146, 2000, pp. 167-184
Selective cyanylation of cysteinyl residues as an approach for the mass spectrometric determination of protein structures
Authors: Barbirz, S Happersberger, HP Przybylski, M Glocker, MO
Citation: S. Barbirz et al., Selective cyanylation of cysteinyl residues as an approach for the mass spectrometric determination of protein structures, EUR MASS SP, 5(2), 1999, pp. 123-131
Identification of linker regions and domain borders of the transcription activator protein NtrC from Escherichia coli by limited proteolysis, in-gel digestion, and mass spectrometry
Authors: Bantscheff, M Weiss, V Glocker, MO
Citation: M. Bantscheff et al., Identification of linker regions and domain borders of the transcription activator protein NtrC from Escherichia coli by limited proteolysis, in-gel digestion, and mass spectrometry, BIOCHEM, 38(34), 1999, pp. 11012-11020
Probing the tertiary structure of multidomain proteins by limited proteolysis and mass spectrometry
Authors: Bantscheff, M Glocker, MO
Citation: M. Bantscheff et Mo. Glocker, Probing the tertiary structure of multidomain proteins by limited proteolysis and mass spectrometry, EUR MASS SP, 4(4), 1998, pp. 279-285
A mass spectrometric approach to the characterization of protein folding reactions
Authors: Happersberger, HP Glocker, MO
Citation: Hp. Happersberger et Mo. Glocker, A mass spectrometric approach to the characterization of protein folding reactions, EUR MASS SP, 4(3), 1998, pp. 209-214
Selective bridging of bis-cysteinyl residues by arsonous acid derivatives as an approach to the characterization of protein tertiary structures and folding pathways by mass spectrometry
Authors: Happersberger, HP Przybylski, M Glocker, MO
Citation: Hp. Happersberger et al., Selective bridging of bis-cysteinyl residues by arsonous acid derivatives as an approach to the characterization of protein tertiary structures and folding pathways by mass spectrometry, ANALYT BIOC, 264(2), 1998, pp. 237-250
Risultati: 1-8 |