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K Kirschner

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Arzneimittel-Forschung|January 1, 1977
[Assembly and function of organized enzymes (author's transl)]K Kirschner
Biochemistry|April 14, 1992
Stable substructures of eightfold beta alpha-barrel proteins: fragment complementation of phosphoribosylanthranilate isomeraseJ Eder, K Kirschner
Biochemistry|September 16, 1980
Kinetics of cooperative ligand binding to the apo beta 2 subunit of tryptophan synthase and its modulation by the alp ha subunitJ Tschopp, K Kirschner
Biochemistry|February 20, 1990
Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediateM Herold, K Kirschner
Protein Science : a Publication of the Protein Society|January 1, 1992
The importance of surface loops for stabilizing an eightfold beta alpha barrel proteinR Urfer, K Kirschner
FEBS Letters|March 13, 1989
Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coliM Eberhard, K Kirschner
Biochemistry|September 16, 1980
Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analoguesJ Tschopp, K Kirschner
Protein Engineering|February 1, 1991
Improving the prediction of secondary structure of 'TIM-barrel' enzymesT Niermann, K Kirschner
Protein Engineering|June 1, 1995
The predicted secondary structure of the G-type glutamine amidotransferase is compatible with TIM-barrel topologyT Niermann, K Kirschner
European Journal of Biochemistry|June 1, 1976
Steady-state kinetic studies of the synthesis of indoleglycerol phosphate catalyzed by the alpha subunit of tryptophan synthase from Escherichia coli. Comparison with the alpha2 beta2-complexW O Weischet, K Kirschner
Pageof 10

Showing results (1-10 of 100) with videos related to

Sort By:
Pageof 10
Arzneimittel-Forschung|January 1, 1977
[Assembly and function of organized enzymes (author's transl)]K Kirschner
Biochemistry|April 14, 1992
Stable substructures of eightfold beta alpha-barrel proteins: fragment complementation of phosphoribosylanthranilate isomeraseJ Eder, K Kirschner
Biochemistry|September 16, 1980
Kinetics of cooperative ligand binding to the apo beta 2 subunit of tryptophan synthase and its modulation by the alp ha subunitJ Tschopp, K Kirschner
Biochemistry|February 20, 1990
Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediateM Herold, K Kirschner
Protein Science : a Publication of the Protein Society|January 1, 1992
The importance of surface loops for stabilizing an eightfold beta alpha barrel proteinR Urfer, K Kirschner
FEBS Letters|March 13, 1989
Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coliM Eberhard, K Kirschner
Biochemistry|September 16, 1980
Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analoguesJ Tschopp, K Kirschner
Protein Engineering|February 1, 1991
Improving the prediction of secondary structure of 'TIM-barrel' enzymesT Niermann, K Kirschner
Protein Engineering|June 1, 1995
The predicted secondary structure of the G-type glutamine amidotransferase is compatible with TIM-barrel topologyT Niermann, K Kirschner
European Journal of Biochemistry|June 1, 1976
Steady-state kinetic studies of the synthesis of indoleglycerol phosphate catalyzed by the alpha subunit of tryptophan synthase from Escherichia coli. Comparison with the alpha2 beta2-complexW O Weischet, K Kirschner
Pageof 10