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- W2515709847 abstract "The affinity and stoichiometry of DNA bind- ing by Escherichia coli trp repressor were studied by electro- phoresis in nondenaturing gels. The ability of trp repressor to retard the electrophoretic mobility of an operator DNA frag- ment depends on the pH of the gel system. Above the p1 of the protein, little retardation of DNA is observed, although com- plex formation can be detected by other assays. As the pH of the gel is lowered, retardation is enhanced. The apparent dissociation constant for the interaction between trp repressor and trpEDCBA operator fragments is 0.5 nM under the conditions used here. Nonspecific binding occurs with only about 200-fold weaker affinity. The stoichiometries of specifiic and nonspecific complexes were determined directly by using tip repressor labeled in vivo. High-affinity operator binding requires a single dimer of tip repressor. DNase I-protection analysis (footprinting) was used to confirm the dissociation constants and to locate the binding site." @default.
- W2515709847 created "2016-09-16" @default.
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- W2515709847 date "2016-01-01" @default.
- W2515709847 modified "2023-09-27" @default.
- W2515709847 title "Gel retardation at low pH resolves trp repressor-DNA complexes for quantitative study (gel pH effects/specific and nonspecific binding/apparent dissociation constant/stoichiometry/cooperativity)" @default.
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