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Biochemistry|January 4, 1983
Polarization of substrate carbonyl groups by yeast aldolase: investigation by Fourier transform infrared spectroscopyJ G Belasco, J R KnowlesBiochemistry|October 26, 1982
Ribulose-1,5-bisphosphate carboxylase: fate of the tritium label in [3]3H]ribulose 1,5-bisphosphate during the enzyme-catalyzed reactionJ M Sue, J R KnowlesBiochemistry|April 27, 1993
Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomeraseP J Lodi, J R KnowlesThe Journal of Biological Chemistry|June 25, 1981
The stereochemical course of the reaction catalyzed by creatine kinaseD E Hansen, J R KnowlesBiochemistry|July 16, 1991
Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implicationsP J Lodi, J R KnowlesThe Journal of Biological Chemistry|December 25, 1982
The stereochemical course at phosphorus of the reaction catalyzed by phosphoenolpyruvate carboxylaseD E Hansen, J R KnowlesBiochemistry|February 5, 1980
Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopyJ G Belasco, J R KnowlesBiochemistry|June 8, 1982
Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acidC J Easton, J R KnowlesThe Biochemical Journal|August 1, 1974
The existence of an electrophilic component in the reaction catalysed by triose phosphate isomeraseM R Webb, J R KnowlesBiochemistry|October 26, 1982
Ribulose-1,5-bisphosphate carboxylase: primary deuterium kinetic isotope effect using [3-2H]ribulose 1,5-bisphosphateJ M Sue, J R KnowlesPageof 16