Quantitative analysis of DNA binding by the Escherichia coli arginine repressor
โ Scribed by Danuta Szwajkajzer; Lizhong Dai; June Wong Fukayama; Bozena Abramczyk; Robert Fairman; Jannette Carey
- Book ID
- 115631279
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 322 KB
- Volume
- 312
- Category
- Article
- ISSN
- 0022-2836
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๐ SIMILAR VOLUMES
NAD(+)-dependent DNA ligases are essential enzymes in bacteria, with the most widely studied of this class of enzymes being LigA from Escherichia coli. NAD(+)-dependent DNA ligases comprise several discrete structural domains, including a BRCT domain at the C-terminus that is highly-conserved in thi
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