Article
Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutant.
Biochemistry - 3 Oct 1995
Li Z, Maki A H, Eftink M R, Mann C J, Matthews C R
Abstract excerpt
The L-tryptophan binding site of the Escherichia coli tryptophan holorepressor (trpR) is characterized by low-temperature phosphorescence and optical detection of magnetic resonance (ODMR) spectroscopy. Measurements are made on a tryptophan-free mutant of trpR, W19/99F, in which both intrinsic tr...
Topics
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Escherichia coli
- Kinetics
- Luminescent Measurements
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Optics and Photonics
- Repressor Proteins
- Tryptophan