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M F Dunn

Showing results (1-10 of 106) with videos related to

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Progress in Clinical and Biological Research|January 1, 1985
The liver alcohol dehydrogenase catalytic mechanism circa 1984M F Dunn
FEMS Microbiology Reviews|September 8, 1998
Tricarboxylic acid cycle and anaplerotic enzymes in rhizobiaM F Dunn
Biochemistry|March 12, 1974
A comparison of the kinetics and stoichiometry of proton uptake with aldehyde reduction for liver alcohol dehydrogenase under single turnover conditionsM F Dunn
Biochemistry|April 16, 1996
beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complexP Pan, M F Dunn
Biochemistry|June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reactionE Woehl, M F Dunn
Biochemistry|June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactionsE Woehl, M F Dunn
Biochemistry|February 11, 1992
Spectroscopic evidence for an intermediate in the T6 to R6 allosteric transition of the Co(II)-substituted insulin hexamerL Gross, M F Dunn
Biochemistry|March 6, 1990
Allosteric effects acting over a distance of 20-25 A in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediatesK F Houben, M F Dunn
Progress in Clinical and Biological Research|January 1, 1985
Native and carboxymethylated horse liver alcohol dehydrogenase: electrostatic fields and the Pauling strain-distortion hypothesisM F Dunn, K H Dahl
Biochemistry|July 25, 1995
Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complexE U Woehl, M F Dunn
Pageof 11

Showing results (1-10 of 106) with videos related to

Sort By:
Pageof 11
Progress in Clinical and Biological Research|January 1, 1985
The liver alcohol dehydrogenase catalytic mechanism circa 1984M F Dunn
FEMS Microbiology Reviews|September 8, 1998
Tricarboxylic acid cycle and anaplerotic enzymes in rhizobiaM F Dunn
Biochemistry|March 12, 1974
A comparison of the kinetics and stoichiometry of proton uptake with aldehyde reduction for liver alcohol dehydrogenase under single turnover conditionsM F Dunn
Biochemistry|April 16, 1996
beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complexP Pan, M F Dunn
Biochemistry|June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reactionE Woehl, M F Dunn
Biochemistry|June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactionsE Woehl, M F Dunn
Biochemistry|February 11, 1992
Spectroscopic evidence for an intermediate in the T6 to R6 allosteric transition of the Co(II)-substituted insulin hexamerL Gross, M F Dunn
Biochemistry|March 6, 1990
Allosteric effects acting over a distance of 20-25 A in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediatesK F Houben, M F Dunn
Progress in Clinical and Biological Research|January 1, 1985
Native and carboxymethylated horse liver alcohol dehydrogenase: electrostatic fields and the Pauling strain-distortion hypothesisM F Dunn, K H Dahl
Biochemistry|July 25, 1995
Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complexE U Woehl, M F Dunn
Pageof 11