Study of cysteine residues in the α subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability

Protein Engineering

Volumn 9, Issue 5, 1996, Pages 425-431

  Hiraga, Kaori ^a   Yutani, Katsuhide ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Calorimetry; Cysteine residue; Denatured structure; Protein stability; Site directed mutagenesis

Indexed keywords

CYSTEINE; MUTANT PROTEIN; TRYPTOPHAN SYNTHASE;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; ARTICLE; CALORIMETRY; CONTROLLED STUDY; ENTHALPY; ENTROPY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME SUBUNIT; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

EID: 0029895252     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/9.5.425     Document Type: Article

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