+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Structure and folding of mutant escherichia coli tryptophan synthase alpha subunits



Structure and folding of mutant escherichia coli tryptophan synthase alpha subunits



Journal of Cellular Biochemistry Suppl. (9 Part B): 95




Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 029224333

Download citation: RISBibTeXText


Related references

Fluorescence and folding properties of Tyr mutant tryptophan synthase alpha-subunits from Escherichia coli. Biochemical and Biophysical Research Communications 300(1): 29-35, 2003

Homodimers of mutant tryptophan synthase alpha-subunits in Escherichia coli. Biochemical and Biophysical Research Communications 289(2): 568-572, 2001

Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. Archives of Biochemistry and Biophysics 292(1): 34-41, 1992

Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits. Journal of Biological Chemistry 266(30): 20205-20212, 1991

Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. Journal of Bacteriology 173(6): 1886-1893, 1991

Substrate interactions with the alpha-subunit of the Escherichia coli tryptophan synthase. A study of the activity of mutant alpha-subunits. Archives of Biochemistry and Biophysics 181(2): 428-437, 1977

Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli. Molecules and Cells 19(2): 219-222, 2005

Enzymatic properties of mutant escherichia coli tryptophan synthase alpha subunits obtained from in vitro mutagenesis of the trp a gene. FASEB Journal 4(7): A1760, 1990

Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase b2 subunits. European Journal of Biochemistry 240: 5-21, 1996

Transient non-native interactions in early folding intermediates do not influence the folding kinetics of Escherichia coli tryptophan synthase beta 2 subunits. European Journal of Biochemistry 240(3): 615-621, 1996

In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant alpha-subunits. Journal of Biological Chemistry 261(35): 16604-16615, 1986

The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Science 8(8): 1623-1635, 1999

Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Journal of Biological Chemistry 270(47): 28177-28182, 1995

Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. Journal of Biological Chemistry 270(30): 17712-5, 1995

Enzymatic properties of mutant Escherichia coli tryptophan synthase a-subunits. The Journal of Biological Chemistry 266: 205-12, 1991