Article
Luminescence studies with trp repressor and its single-tryptophan mutants.
Biochemistry - 7 Sept 1993
Eftink M R, Ramsay G D, Burns L, Maki A H, Mann C J, Matthews C R, Ghiron C A
Abstract excerpt
Time-resolved and steady-state fluorescence, low-temperature phosphorescence, and optically detected magnetic resonance (ODMR) measurements have been made to resolve the luminescence contributions of the two intrinsic tryptophan residues in the subunits of trp aporepressor from Escherichia coli....
Topics
- Apoproteins
- Bacterial Proteins
- Cold Temperature
- Energy Transfer
- Escherichia coli
- Escherichia coli Proteins
- Fluorescence
- Luminescent Measurements
- Magnetic Resonance Spectroscopy
- Models, Chemical
- Mutation
- Potassium Iodide
- Recombinant Proteins
- Repressor Proteins
- Spectrometry, Fluorescence
- Structure-Activity Relationship
- Time Factors
- Tryptophan