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Progress in Clinical and Biological Research
|
January 1, 1985
The liver alcohol dehydrogenase catalytic mechanism circa 1984
M F Dunn
FEMS Microbiology Reviews
|
September 8, 1998
Tricarboxylic acid cycle and anaplerotic enzymes in rhizobia
M 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 conditions
M F Dunn
Biochemistry
|
April 16, 1996
beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex
P Pan, M F Dunn
Biochemistry
|
June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction
E Woehl, M F Dunn
Biochemistry
|
June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions
E 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 hexamer
L 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 intermediates
K 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 hypothesis
M 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 complex
E U Woehl, M F Dunn
Page
of 11
Search research articles
Search
Showing results (1-10 of 106) with videos related to
Sort By:
Page
of 11
Progress in Clinical and Biological Research
|
January 1, 1985
The liver alcohol dehydrogenase catalytic mechanism circa 1984
M F Dunn
FEMS Microbiology Reviews
|
September 8, 1998
Tricarboxylic acid cycle and anaplerotic enzymes in rhizobia
M 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 conditions
M F Dunn
Biochemistry
|
April 16, 1996
beta-Site covalent reactions trigger transitions between open and closed conformations of the tryptophan synthase bienzyme complex
P Pan, M F Dunn
Biochemistry
|
June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the first stage of the tryptophan synthase beta-reaction
E Woehl, M F Dunn
Biochemistry
|
June 3, 1999
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions
E 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 hexamer
L 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 intermediates
K 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 hypothesis
M 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 complex
E U Woehl, M F Dunn
Page
of 11