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The Journal of Biological Chemistry
|
June 25, 1988
Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit
E W Miles, P McPhie, K Yutani
Archives of Biochemistry and Biophysics
|
January 1, 1991
Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase alpha subunit from Salmonella typhimurium
H Kanzaki, P McPhie, E W Miles
Biochemistry
|
May 25, 1982
Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains
E W Miles, K Yutani, K Ogasahara
Biochemistry
|
July 29, 1986
Beta-elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: a comparison between reactions catalyzed by tryptophanase and tryptophan synthase
S A Ahmed, B Martin, E W Miles
Biochemistry
|
July 1, 1999
Guanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation
Y X Fan, P McPhie, E W Miles
The Journal of Biological Chemistry
|
April 15, 1989
The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site
S Nagata, C C Hyde, E W Miles
The Journal of Biological Chemistry
|
May 16, 1998
Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49
S Rhee, E W Miles, D R Davies
The Journal of Biological Chemistry
|
November 15, 1996
Mechanism of activation of the tryptophan synthase alpha2beta2 complex. Solvent effects of the co-substrate beta-mercaptoethanol
S A Ahmed, P McPhie, E W Miles
Biochemistry
|
April 19, 2000
Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects
Y X Fan, P McPhie, E W Miles
Biochemistry
|
August 24, 2000
Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation
K H Jhee, P McPhie, E W Miles
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of 9
Search research articles
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Showing results (21-30 of 83) with videos related to
Sort By:
Page
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The Journal of Biological Chemistry
|
June 25, 1988
Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit
E W Miles, P McPhie, K Yutani
Archives of Biochemistry and Biophysics
|
January 1, 1991
Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase alpha subunit from Salmonella typhimurium
H Kanzaki, P McPhie, E W Miles
Biochemistry
|
May 25, 1982
Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains
E W Miles, K Yutani, K Ogasahara
Biochemistry
|
July 29, 1986
Beta-elimination of indole from L-tryptophan catalyzed by bacterial tryptophan synthase: a comparison between reactions catalyzed by tryptophanase and tryptophan synthase
S A Ahmed, B Martin, E W Miles
Biochemistry
|
July 1, 1999
Guanidine hydrochloride exerts dual effects on the tryptophan synthase alpha 2 beta 2 complex as a cation activator and as a modulator of the active site conformation
Y X Fan, P McPhie, E W Miles
The Journal of Biological Chemistry
|
April 15, 1989
The alpha subunit of tryptophan synthase. Evidence that aspartic acid 60 is a catalytic residue and that the double alteration of residues 175 and 211 in a second-site revertant restores the proper geometry of the substrate binding site
S Nagata, C C Hyde, E W Miles
The Journal of Biological Chemistry
|
May 16, 1998
Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49
S Rhee, E W Miles, D R Davies
The Journal of Biological Chemistry
|
November 15, 1996
Mechanism of activation of the tryptophan synthase alpha2beta2 complex. Solvent effects of the co-substrate beta-mercaptoethanol
S A Ahmed, P McPhie, E W Miles
Biochemistry
|
April 19, 2000
Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects
Y X Fan, P McPhie, E W Miles
Biochemistry
|
August 24, 2000
Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation
K H Jhee, P McPhie, E W Miles
Page
of 9