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J R Knowles

Showing results (31-40 of 167) with videos related to

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Biochemistry|December 14, 1976
Evolution of enzyme function and the development of catalytic efficiencyW J Albery, J R Knowles
Journal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. I. Isotopic experiments, enzyme interconversion, and oversaturationW J Albery, J R Knowles
Journal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviourW J Albery, J R Knowles
Nucleic Acids Research|March 11, 1985
A simple and efficient method for chemical mutagenesis of DNAJ T Kadonaga, J R Knowles
Biochemistry|May 10, 1994
Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active siteH M Seidel, J R Knowles
Biochemistry|November 28, 1989
Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinaseJ J Burbaum, J R Knowles
Angewandte Chemie (International Ed. in English)|May 1, 1977
Efficiency and evolution of enzyme catalysisW J Albery, J R Knowles
Biochemistry|November 3, 1987
Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: detection and kinetic characterization of two unliganded forms of the enzymeR T Raines, J R Knowles
Biochemistry|July 16, 1991
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implicationsP J Lodi, J R Knowles
The Journal of Biological Chemistry|December 25, 1982
The stereochemical course at phosphorus of the reaction catalyzed by phosphoenolpyruvate carboxylaseD E Hansen, J R Knowles
Pageof 17

Showing results (31-40 of 167) with videos related to

Sort By:
Pageof 17
Biochemistry|December 14, 1976
Evolution of enzyme function and the development of catalytic efficiencyW J Albery, J R Knowles
Journal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. I. Isotopic experiments, enzyme interconversion, and oversaturationW J Albery, J R Knowles
Journal of Theoretical Biology|January 21, 1987
Energetics of enzyme catalysis. II. Oversaturation, case diagrams, reversible and irreversible behaviourW J Albery, J R Knowles
Nucleic Acids Research|March 11, 1985
A simple and efficient method for chemical mutagenesis of DNAJ T Kadonaga, J R Knowles
Biochemistry|May 10, 1994
Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active siteH M Seidel, J R Knowles
Biochemistry|November 28, 1989
Internal thermodynamics of enzymes determined by equilibrium quench: values of Kint for enolase and creatine kinaseJ J Burbaum, J R Knowles
Angewandte Chemie (International Ed. in English)|May 1, 1977
Efficiency and evolution of enzyme catalysisW J Albery, J R Knowles
Biochemistry|November 3, 1987
Enzyme relaxation in the reaction catalyzed by triosephosphate isomerase: detection and kinetic characterization of two unliganded forms of the enzymeR T Raines, J R Knowles
Biochemistry|July 16, 1991
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implicationsP J Lodi, J R Knowles
The Journal of Biological Chemistry|December 25, 1982
The stereochemical course at phosphorus of the reaction catalyzed by phosphoenolpyruvate carboxylaseD E Hansen, J R Knowles
Pageof 17