+ 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

Folding of mutant tryptophan synthase alpha subunit proteins



Folding of mutant tryptophan synthase alpha subunit proteins



Federation Proceedings 45(6): 1919




Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 028347798

Download citation: RISBibTeXText


Related references

Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. Biochemistry 25(21): 6356-6360, 1986

Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. Biochemistry 27(2): 824-832, 1988

Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. International Journal of Peptide and Protein Research 20(4): 331-336, 1982

Calorimetric study of tryptophan synthase alpha subunit and 2 mutant proteins. International Journal of Peptide & Protein Research 20(4): 331-336, 1982

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. Journal of Biological Chemistry 263(18): 8611-8614, 1988

PH dependence of stability of the wild-type tryptophan synthase alpha-subunit and two mutant proteins (Glu49 replaced by Met or Gln). Journal of Molecular Biology 144(4): 455-465, 1980

Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry 38(31): 10205-10214, 1999

Synergism in folding of a double mutant of the a subunit of tryptophan synthase. Biochemistry (American Chemical Society) 25: 56-60, 1986

Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. Biochemistry 44(4): 1184-1192, 2005

Ph dependence of stability of the wild type tryptophan synthase alpha subunit and 2 mutant proteins glutamic acid 49 methionine or glutamine. Journal of Molecular Biology 144(4): 455-466, 1980

Folding of homologous proteins: conservation of the folding mechanism of the a subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. Biochemistry (American Chemical Society) 27: 4-32, 1988

Effect of amino acid residues on conformational stability in eight mutant proteins variously substituted at a unique position of the tryptophan synthase alpha-subunit. Journal of Biological Chemistry 259(22): 14076-14081, 1984

Stable intermediates in the folding of the alpha subunit of tryptophan synthase. Biophysical Journal 33(2 Part 2): 260A, 1981

Characterization of the amino folding unit of the alpha subunit of tryptophan synthase. Biophysical Journal 64(2 Part 2): A173, 1993

Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase. Proteins 2(1): 54-63, 1987