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J R Knowles

Showing results (151-160 of 167) with videos related to

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Proceedings of the National Academy of Sciences of the United States of America|May 1, 1978
Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinaseG A Orr, J Simon, S R Jones, et al.
Biochemistry|November 4, 1986
Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartateR T Raines, E L Sutton, D R Straus, et al.
Biochemistry|January 22, 1980
Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O]phosphoryl groupD H Pliura, D Schomburg, J P Richard, et al.
Gene|December 7, 1989
A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primersJ D Hermes, S M Parekh, S C Blacklow, et al.
The Journal of Biological Chemistry|December 15, 1991
Ligand recognition by influenza virus. The binding of bivalent sialosidesG D Glick, P L Toogood, D C Wiley, et al.
Biochemistry|May 6, 1986
Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic stepsL M Fisher, J G Belasco, T W Bruice, et al.
Biochemistry|June 28, 1988
Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphataseJ E Butler-Ransohoff, D A Kendall, S Freeman, et al.
Biochemistry|May 6, 1986
Energetics of proline racemase: rates, fractionation factors, and buffer catalysis in the oversaturated region. Nature of the interconversion of the two forms of free enzymeJ G Belasco, T W Bruice, L M Fisher, et al.
Biochemistry|February 23, 1988
Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMRS C Blacklow, R T Raines, W A Lim, et al.
The Biochemical Journal|September 1, 1972
Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosineS De la Mare, A F Coulson, J R Knowles, et al.
Pageof 17

Showing results (151-160 of 167) with videos related to

Sort By:
Pageof 17
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1978
Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinaseG A Orr, J Simon, S R Jones, et al.
Biochemistry|November 4, 1986
Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartateR T Raines, E L Sutton, D R Straus, et al.
Biochemistry|January 22, 1980
Stereochemical course of a phosphokinase using a chiral [18O]phosphorothioate. Comparison with the transfer of a chiral [16O,17O,18O]phosphoryl groupD H Pliura, D Schomburg, J P Richard, et al.
Gene|December 7, 1989
A reliable method for random mutagenesis: the generation of mutant libraries using spiked oligodeoxyribonucleotide primersJ D Hermes, S M Parekh, S C Blacklow, et al.
The Journal of Biological Chemistry|December 15, 1991
Ligand recognition by influenza virus. The binding of bivalent sialosidesG D Glick, P L Toogood, D C Wiley, et al.
Biochemistry|May 6, 1986
Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic stepsL M Fisher, J G Belasco, T W Bruice, et al.
Biochemistry|June 28, 1988
Stereochemistry of phospho group transfer catalyzed by a mutant alkaline phosphataseJ E Butler-Ransohoff, D A Kendall, S Freeman, et al.
Biochemistry|May 6, 1986
Energetics of proline racemase: rates, fractionation factors, and buffer catalysis in the oversaturated region. Nature of the interconversion of the two forms of free enzymeJ G Belasco, T W Bruice, L M Fisher, et al.
Biochemistry|February 23, 1988
Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMRS C Blacklow, R T Raines, W A Lim, et al.
The Biochemical Journal|September 1, 1972
Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosineS De la Mare, A F Coulson, J R Knowles, et al.
Pageof 17