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Volumn 40, Issue 51, 2001, Pages 15650-15659

Engineered disulfide linking the hinge regions within lactose repressor dimer increases operator affinity, decreases sequence selectivity, and alters allostery

(2) Falcon, C M a,b Matthews, K S a

a RICE UNIVERSITY (United States)

b Tanox Biosystems Inc (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY;

AMINO ACIDS; CHEMICAL BONDS; CONFORMATIONS; DIMERS; DNA; MUTAGENESIS;

BIOCHEMISTRY;

AMINO ACID; DIMER; DISULFIDE; DNA; LACTOSE; REPRESSOR PROTEIN;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; DNA BINDING; DNA SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DNA INTERACTION;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BASE PAIRING; BASE SEQUENCE; BINDING SITES; CYSTEINE; DIMERIZATION; DISULFIDES; DNA, BACTERIAL; ESCHERICHIA COLI PROTEINS; GENETIC VECTORS; MUTAGENESIS, SITE-DIRECTED; OPERATOR REGIONS (GENETICS); PROTEIN BINDING; REPRESSOR PROTEINS; TEMPERATURE; VALINE;

EID: 0035951105 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0114067 Document Type: Article

Times cited : (30)

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