Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator

Journal of Molecular Biology

Volumn 313, Issue 1, 2001, Pages 99-109

  Bell, Charles E ^a   Barry, Jennifer ^b   Matthews, Kathleen S ^b   Lewis, Mitchell ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b RICE UNIVERSITY   (United States)

Author keywords

Allosteric transition; DNA binding proteins; lac repressor; Protein folding; Protein stability

Indexed keywords

DIMER; DNA BINDING PROTEIN; GENE PRODUCT; LAC PROTEIN; LEUCINE; LYSINE; MONOMER; REPRESSOR PROTEIN; SOLVENT; TETRAMER; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CHEMICAL BOND; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRICITY; ESCHERICHIA COLI; HYDROGEN BOND; IN VIVO STUDY; NONHUMAN; OPERATOR GENE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN VARIANT; REPRESSOR GENE; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

EID: 0035850794     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5041     Document Type: Article

References (25)

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