Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase α subunit from Salmonella typhimurium-Reference-Cited by-同舟云学术

Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase α subunit from Salmonella typhimurium

Published:1991-01 Issue:1 Volume:284 Page:174-180
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Kanzaki Hiroshi,McPhie Peter,Miles Edith Wilson

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference44 articles.

1. Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions

2. Prediction of secondary structure by evolutionary comparison: Application to the α subunit of tryptophan synthase

3. Tryptophan Biosynthesis in Escherichia coli

Cited by 16 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Stability for Function Trade-Offs in the Enolase Superfamily “Catalytic Module”,;Biochemistry;2007-05-16

2. The PD...(D/E)XK Motif in Restriction Enzymes: A Link between Function and Conformation;Biochemistry;2000-12-20

3. Thermal Repair of Tryptophan Synthase Mutations in a Regulatory Intersubunit Salt Bridge;Journal of Biological Chemistry;2000-07

4. Contribution of the Hydrogen-Bond Network Involving a Tyrosine Triad in the Active Site to the Structure and Function of a Highly Proficient Ketosteroid Isomerase from Pseudomonas putida Biotype B,;Biochemistry;2000-03-28

5. Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1998-04