Refolding mechanism of ovalbumin. Investigation by using a starting urea-denatured disulfide isomer with mispaired Cys367-Cys382

Journal of Biological Chemistry

Volumn 278, Issue 26, 2003, Pages 23600-23609

  Onda, Maki ^a   Hirose, Masaaki ^b  

^a Osaka City University   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDITY; CARBOXYLATION; CONFORMATIONS; HYDROPHOBICITY; PROTEINS; SULFUR COMPOUNDS; UREA;

CARBOXYMETHYLATION;

ISOMERS;

CYSTEINE; DISULFIDE; OVALBUMIN; UREA;

ANTIGEN BINDING; ARTICLE; CIRCULAR DICHROISM; DENATURATION; DILUTION; ISOMER; METHYLATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CHICKENS; CYSTINE; ISOMERISM; KINETICS; OVALBUMIN; PEPTIDE MAPPING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN RENATURATION; UREA;

EID: 0038268512     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M300295200     Document Type: Article

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