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E W Miles

Showing results (51-60 of 83) with videos related to

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The Journal of Biological Chemistry|July 21, 1995
Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A)S B Ruvinov, S A Ahmed, P McPhie, et al.
Biochemistry|October 17, 1998
Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivationK H Jhee, P McPhie, H S Ro, et al.
Biochemistry|June 20, 2001
Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificityD Ferrari, L H Yang, E W Miles, et al.
Biochemistry|August 25, 1987
Microcrystals of tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium are catalytically activeS A Ahmed, C C Hyde, G Thomas, et al.
The Journal of Biological Chemistry|November 15, 1991
Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunitS A Ahmed, S B Ruvinov, A M Kayastha, et al.
Biochemistry|July 29, 1986
Isomerization of (3S)-2,3-dihydro-5-fluoro-L-tryptophan and of 5-fluoro-L-tryptophan catalyzed by tryptophan synthase: studies using fluorine-19 nuclear magnetic resonance and difference spectroscopyE W Miles, R S Phillips, H J Yeh, et al.
Biochemistry|June 3, 1986
Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the beta 2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimuriumS A Ahmed, T Fairwell, S Dunn, et al.
Biochemistry|October 5, 1993
Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesisP S Brzović, C C Hyde, E W Miles, et al.
Biochemistry|February 4, 1992
Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimuriumP S Brzović, A M Kayastha, E W Miles, et al.
The Journal of Social Psychology|January 1, 1999
The importance of employee demographic profiles for understanding experiences of work-family interrole conflictsB W Eagle, M L Icenogle, J D Maes, et al.
Pageof 9

Showing results (51-60 of 83) with videos related to

Sort By:
Pageof 9
The Journal of Biological Chemistry|July 21, 1995
Monovalent cations partially repair a conformational defect in a mutant tryptophan synthase alpha 2 beta 2 complex (beta-E109A)S B Ruvinov, S A Ahmed, P McPhie, et al.
Biochemistry|October 17, 1998
Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivationK H Jhee, P McPhie, H S Ro, et al.
Biochemistry|June 20, 2001
Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificityD Ferrari, L H Yang, E W Miles, et al.
Biochemistry|August 25, 1987
Microcrystals of tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium are catalytically activeS A Ahmed, C C Hyde, G Thomas, et al.
The Journal of Biological Chemistry|November 15, 1991
Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunitS A Ahmed, S B Ruvinov, A M Kayastha, et al.
Biochemistry|July 29, 1986
Isomerization of (3S)-2,3-dihydro-5-fluoro-L-tryptophan and of 5-fluoro-L-tryptophan catalyzed by tryptophan synthase: studies using fluorine-19 nuclear magnetic resonance and difference spectroscopyE W Miles, R S Phillips, H J Yeh, et al.
Biochemistry|June 3, 1986
Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the beta 2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimuriumS A Ahmed, T Fairwell, S Dunn, et al.
Biochemistry|October 5, 1993
Characterization of the functional role of a flexible loop in the alpha-subunit of tryptophan synthase from Salmonella typhimurium by rapid-scanning, stopped-flow spectroscopy and site-directed mutagenesisP S Brzović, C C Hyde, E W Miles, et al.
Biochemistry|February 4, 1992
Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimuriumP S Brzović, A M Kayastha, E W Miles, et al.
The Journal of Social Psychology|January 1, 1999
The importance of employee demographic profiles for understanding experiences of work-family interrole conflictsB W Eagle, M L Icenogle, J D Maes, et al.
Pageof 9