A free cysteine residue at the dimer interface decreases conformational stability of Xenopus laevis copper,zinc superoxide dismutase

Archives of Biochemistry and Biophysics

Volumn 377, Issue 2, 2000, Pages 284-289

  Carmela Bonaccorsi Di Patti, Maria ^b   Carri, Maria Teresa ^a   Gabbianelli, Roberta ^a   Da Gai, Roberto ^c   Volpe, Corrado ^c   Giartosio, Anna ^b   Rotilio, Giuseppe ^a   Battistoni, Andrea ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c ISTITUTO SUPERIORE DI SANITÀ   (Italy)

Author keywords

Differential scanning calorimetry; Protein stability; Protein unfolding; Site directed mutagenesis; Superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; CYSTEINE; DIMER;

ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE BOND; ENZYME CONFORMATION; ENZYME STABILITY; HEAT SENSITIVITY; MELTING POINT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; XENOPUS LAEVIS;

XENOPUS LAEVIS;

EID: 0342859344     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.2000.1786     Document Type: Article

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