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...
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