Effect of Substituted Residue 139 and 258 on Structural Changes of Mutant Tryptophan Synthase Pro96→Leu α-Subunit |
Lee, Joo-Youn
(Department of Molecular Biology, College of Natural Sciences, Pusan National University)
Jeong, Jae-Kap (Department of Molecular Biology, College of Natural Sciences, Pusan National University) Shin, Hae-Ja (Environmental Engineering Major, Division of Applied Engineering, Dongseo University) Lim, Woon-Ki (Department of Molecular Biology, College of Natural Sciences, Pusan National University) |
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Kinetic studies of tryptophan synthase.Interactin of substrates with β subunit
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DOI ScienceOn |
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Site-directed mutagenesis of the β subunit of tryptophan synthase from Salomonella typhimurium
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Guanidine hydrochloride induceed unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments :evidence for stepwise unfolding of th two alpha domains
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DOI ScienceOn |
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Affinities of phosphylated substrates for the E.coli tryptophan synthase alpha-subunit:roles of Ser-235 and helix-8' dipole
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DOI ScienceOn |
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A rapid method for preparing crystalline β2 subunit of trytophan synthase of Escherichia coli in high yied
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An active proteolytic derivation of the alpha submit of tryptophan synthase.Indentificaiton of the site of cleavage and characterization of fragment.
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In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant alpha subunits
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Synergism in folding of double mutant of the α subunit of tryptophan synthase
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DOI ScienceOn |
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The tryptophan synthase from Escherichia coli.An improved purification procedure for the alpha subunit and binding studies with substrate analogues
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DOI ScienceOn |
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Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subinit
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Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmomella typhimurium
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In vivo pathways of degradation and strategies fot protein stabilization
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Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase Enzymatic and urea stability properties
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Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase
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DOI |