A single dipeptide sequence modulates the redox properties of a whole enzyme family

Folding and Design

Volumn 3, Issue 3, 1998, Pages 161-171

  Huber Wunderlich, Martina ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Cys X X Cys motif; DsbA; pK(a) values; Radox potential; Thiol disulfide oxidoreductases

Indexed keywords

CYSTEINE; DIPEPTIDE; DISULFIDE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; THIOL GROUP; THIOREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STABILITY; ESCHERICHIA COLI; OXIDATION REDUCTION POTENTIAL; PKA; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING;

ESCHERICHIA COLI; EUKARYOTA;

EID: 0031776171     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00024-8     Document Type: Article

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