Oxidized GroEL can function as a chaperonin

Frontiers in Bioscience

Volumn 9, Issue , 2004, Pages 724-731

  Melkani, Girish C ^a   Zardeneta, Gustavo ^b   Mendoza, Jose A ^a  

^a CALIFORNIA STATE UNIVERSITY   (United States)

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

Author keywords

Chaperonin; GroEL; Hydrogen Peroxide; Oxidative Stress; Protein Protein Interaction; Reactivation; Rhodanese

Indexed keywords

CHAPERONIN; HYDROGEN PEROXIDE; THIOSULFATE SULFURTRANSFERASE; TRYPTOPHAN; TRYPSIN;

ARTICLE; CENTRIFUGATION; CIRCULAR DICHROISM; COMPLEX FORMATION; ENZYME ACTIVATION; ENZYME INACTIVATION; FLUORESCENCE; HYDROPHOBICITY; OXIDATION; OXIDATIVE STRESS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; STATISTICAL SIGNIFICANCE; STRUCTURE ANALYSIS; SURFACE PROPERTY; ANIMAL; CATTLE; CHEMISTRY; DRUG EFFECT; ESCHERICHIA COLI; METABOLISM; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE;

ANIMALS; CATTLE; CHAPERONINS; ENZYME ACTIVATION; ESCHERICHIA COLI; GROEL PROTEIN; HYDROGEN PEROXIDE; HYDROPHOBICITY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; THIOSULFATE SULFURTRANSFERASE; TRYPSIN;

EID: 2542447201     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1258     Document Type: Article

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