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M D Toney

Showing results (11-20 of 25) with videos related to

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Science (New York, N.Y.)|March 17, 1989
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous aminesM D Toney, J F Kirsch
Biochemistry|May 16, 1998
Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ionsX Zhou, S Kay, M D Toney
Protein Science : a Publication of the Protein Society|November 1, 1995
Active site model for gamma-aminobutyrate aminotransferase explains substrate specificity and inhibitor reactivitiesM D Toney, S Pascarella, D De Biase
Biochemistry|April 2, 1998
Reactions of alternate substrates demonstrate stereoelectronic control of reactivity in dialkylglycine decarboxylaseS Sun, R F Zabinski, M D Toney
Biochemistry|April 2, 1998
Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylaseS Sun, C K Bagdassarian, M D Toney
Biochemistry|December 14, 1993
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferaseV N Malashkevich, M D Toney, J N Jansonius
Biochemistry|May 2, 1989
Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solventD A Julin, H Wiesinger, M D Toney, et al.
Science (New York, N.Y.)|August 6, 1993
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sitesM D Toney, E Hohenester, S W Cowan, et al.
Journal of Molecular Biology|January 13, 1995
Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylaseM D Toney, E Hohenester, J W Keller, et al.
Biochemistry|October 3, 1989
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coliD L Smith, S C Almo, M D Toney, et al.
Pageof 3

Showing results (11-20 of 25) with videos related to

Sort By:
Pageof 3
Science (New York, N.Y.)|March 17, 1989
Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous aminesM D Toney, J F Kirsch
Biochemistry|May 16, 1998
Coexisting kinetically distinguishable forms of dialkylglycine decarboxylase engendered by alkali metal ionsX Zhou, S Kay, M D Toney
Protein Science : a Publication of the Protein Society|November 1, 1995
Active site model for gamma-aminobutyrate aminotransferase explains substrate specificity and inhibitor reactivitiesM D Toney, S Pascarella, D De Biase
Biochemistry|April 2, 1998
Reactions of alternate substrates demonstrate stereoelectronic control of reactivity in dialkylglycine decarboxylaseS Sun, R F Zabinski, M D Toney
Biochemistry|April 2, 1998
Pre-steady-state kinetic analysis of the reactions of alternate substrates with dialkylglycine decarboxylaseS Sun, C K Bagdassarian, M D Toney
Biochemistry|December 14, 1993
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferaseV N Malashkevich, M D Toney, J N Jansonius
Biochemistry|May 2, 1989
Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solventD A Julin, H Wiesinger, M D Toney, et al.
Science (New York, N.Y.)|August 6, 1993
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sitesM D Toney, E Hohenester, S W Cowan, et al.
Journal of Molecular Biology|January 13, 1995
Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylaseM D Toney, E Hohenester, J W Keller, et al.
Biochemistry|October 3, 1989
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coliD L Smith, S C Almo, M D Toney, et al.
Pageof 3