Thermodynamic Analysis of Small Ligand Binding to the Escherichia coli Repressor of Biotin Biosynthesis †
✍ Scribed by Xu, Yan; Johnson, Craig R.; Beckett, Dorothy
- Book ID
- 127001473
- Publisher
- American Chemical Society
- Year
- 1996
- Tongue
- English
- Weight
- 544 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-2960
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Equilibrium binding of Escherichia coli LexA repressor to the recA operator was studied by the polyacrylamide gel mobility shift assay as a function of solution conditions. In the presence of NsCl at 20"C, there was a significant salt dependence in binding to the recA operator, typical for protein-n
In the lac operon, the existence of a secondary repressor binding site, inside Z gene, had been inferred from in vitro binding studies (Reznikoff et al., 1974; Gilbert et al., 1975). A series of deletions have been constructed from a lac transducing lambda bacteriophage. Some of those deleted bacter