Article
Design and evaluation of a tryptophanless RecA protein with wild type activity.
Biochemical and biophysical research communications - 7 Sept 2001
Berger M D, Lee A M, Simonette R A, Jackson B E, Roca A I, Singleton S F
Abstract excerpt
The C-terminal domain of the Escherichia coli RecA protein contains two tryptophan residues whose native fluorescence emission provides an interfering background signal when other fluorophores such as 1,N(6)-ethenoadenine, 2-aminopurine and other tryptophan residues are used to probe the protein's activities. Replacement of the wild type tryptophans with nonfluorescent residues is not trivial because one...
Topics
- 2-Aminopurine
- Adenine
- Cell Survival
- DNA
- DNA, Single-Stranded
- Dose-Response Relationship, Radiation
- Electrophoresis, Polyacrylamide Gel
- Hydrolysis
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutagens