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Volumn 278, Issue 49, 2003, Pages 49478-49486
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Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins.
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Author keywords
[No Author keywords available]
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Indexed keywords
DISULFIDE;
ESCHERICHIA COLI PROTEIN;
PERIPLASMIC PROTEIN;
PEROXIDASE;
TPX PROTEIN, E COLI;
AMINO ACID SEQUENCE;
ARTICLE;
CHEMICAL STRUCTURE;
CHEMISTRY;
ENZYME SPECIFICITY;
ENZYMOLOGY;
ESCHERICHIA COLI;
METABOLISM;
MOLECULAR GENETICS;
OXIDATION REDUCTION REACTION;
PROTEIN CONFORMATION;
SEQUENCE HOMOLOGY;
X RAY CRYSTALLOGRAPHY;
AMINO ACID SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
DISULFIDES;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
OXIDATION-REDUCTION;
PERIPLASMIC PROTEINS;
PEROXIDASES;
PROTEIN CONFORMATION;
SEQUENCE HOMOLOGY, AMINO ACID;
SUBSTRATE SPECIFICITY;
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EID: 1542272169
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M309015200 Document Type: Article |
Times cited : (59)
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References (0)
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