Thermal denaturation of tryptophan synthase α-subunit
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1984.tb00940.x/fullpdf
Reference18 articles.
1. The Stability of Globular Protein
2. Thermal investigations of biopolymer solutions and scanning microcalorimetry
3. Stability of Proteins Small Globular Proteins
4. Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)
5. Effect of single amino acid substitutions at the same position on stability of a two-domain protein
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1. A New Method for the Determination of Stability Parameters of Proteins from Their Heat-Induced Denaturation Curves;Analytical Biochemistry;2000-08
2. Tryptophan Synthase;Subcellular Biochemistry;1995
3. Thermal inactivation of tryptophan synthase. Stabilization by protein-protein interaction and protein-ligand interaction.;Journal of Biological Chemistry;1994-04
4. Role of conserved proline residues in stabilizing tryptophan synthase α subunit: Analysis by mutants with alanine or glycine;Proteins: Structure, Function, and Genetics;1991-02
5. Effect of single amino acid substitutions at positions 49 and 60 on the thermal unfolding of the tryptophan synthase α subunit from Salmonella typhimurium;Archives of Biochemistry and Biophysics;1991-01
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