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J F Kirsch

Showing results (1-10 of 67) with videos related to

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Biochemistry|March 8, 2000
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthaseL Feng, J F Kirsch
Biochemistry|May 26, 1981
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 1. beta-galactosidease-catalyzed hydrolysisS Rosenberg, J F Kirsch
Biochemistry|May 26, 1981
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysisS Rosenberg, J F Kirsch
Biochemistry|February 13, 1996
Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysisI Matsumura, J F Kirsch
Proteins|May 17, 2000
Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complexA Rajpal, J F Kirsch
Protein Engineering|July 1, 1990
Sequential protection-modification method for selective sulfhydryl group derivatization in proteins having more than one cysteineA Planas, J F Kirsch
Biochemistry|August 20, 1991
Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteineA Planas, J F Kirsch
Biochemistry|February 13, 1996
Synergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozymeI Matsumura, J F Kirsch
Protein Science : a Publication of the Protein Society|October 1, 1995
Design and structural analysis of an engineered thermostable chicken lysozymeP Shih, J F Kirsch
Biochemistry|March 1, 1984
Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase IL W Hardy, J F Kirsch
Pageof 7

Showing results (1-10 of 67) with videos related to

Sort By:
Pageof 7
Biochemistry|March 8, 2000
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthaseL Feng, J F Kirsch
Biochemistry|May 26, 1981
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 1. beta-galactosidease-catalyzed hydrolysisS Rosenberg, J F Kirsch
Biochemistry|May 26, 1981
Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysisS Rosenberg, J F Kirsch
Biochemistry|February 13, 1996
Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysisI Matsumura, J F Kirsch
Proteins|May 17, 2000
Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complexA Rajpal, J F Kirsch
Protein Engineering|July 1, 1990
Sequential protection-modification method for selective sulfhydryl group derivatization in proteins having more than one cysteineA Planas, J F Kirsch
Biochemistry|August 20, 1991
Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteineA Planas, J F Kirsch
Biochemistry|February 13, 1996
Synergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozymeI Matsumura, J F Kirsch
Protein Science : a Publication of the Protein Society|October 1, 1995
Design and structural analysis of an engineered thermostable chicken lysozymeP Shih, J F Kirsch
Biochemistry|March 1, 1984
Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase IL W Hardy, J F Kirsch
Pageof 7