NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions

Journal of Biological Chemistry

Volumn 274, Issue 20, 1999, Pages 13938-13947

  Trevino, Richard J ^a   Gliubich, Francesca ^b,c   Berni, Rodolfo ^d   Cianci, Michele ^b   Chirgwin, John M ^a   Zanotti, Giuseppe ^b   Horowitz, Paul M ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^b UNIVERSITY OF PADOVA   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

^d UNIVERSITY OF PARMA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

THIOSULFATE SULFURTRANSFERASE; CHAPERONIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CATTLE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; ANIMAL; CHEMICAL STRUCTURE; COMPARATIVE STUDY; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

ANIMALS; CATTLE; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GROEL PROTEIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; THIOSULFATE SULFURTRANSFERASE;

EID: 0033553215     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.20.13938     Document Type: Article

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