The intrinsic steady-state fluorescence and fluorescence decay of Staphylococcus epidermidis, Pseudomonas fluorescens, Enterobacter cloacae, Escherichia coli, and Bacillus subtilis have been observed. Each organism exhibits a strong maximum in its emission spectrum at 330-340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 330-340-nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein-tryptophan fluorescence has been described by two exponential functions in all cases
Double-exponential decay has been observed for tryptophan and tryptophan-containing dipeptides. The ...
The fluorescence properties of neutral protease from B. subtilis have been investigated under a vari...
<p>Fluorescence emission of each protein collected at 0.20–0.33 mg/ml in 50 mM sodium phosphate, pH ...
The UV photodissociation kinetics of tryptophan amino acid, Trp, attached to the membrane of bacteri...
The decay of the tryptophanyl emission in proteins is often complex due to the sensitivity of the tr...
The decay of the tryptophanyl emission in proteins is often complex due to the sensitivity of the tr...
The intrinsic steady-state fluorescence and fluoresence decay of Staphylococcus epidermidis, Psuedom...
Time correlated single photon counting measurements of tryptophan (Trp) fluorescence intensity decay...
The picosecond time-resolved fluorescence decay of bacteriorhodopsin (BR) was analyzed by the maximu...
The fluorescence of the single tryptophan in Bacillus stearothermophilus phosphofructokinase was cha...
<p>Tryptophan fluorescence spectra of different samples (0.1 mg/ml protein) were recorded from 310–4...
AbstractA power-like decay function, characterized by the mean excited-state lifetime and relative v...
The fluorescence and phosphorescence spectra of model indole compounds and of cod parvalbumin III, a...
most probable spectral classes of emitting tryptophan residues and differences among the classes wer...
The time-resolved fluorescence properties of the bacteriophage T4 capsid protein gp23 are investigat...
Double-exponential decay has been observed for tryptophan and tryptophan-containing dipeptides. The ...
The fluorescence properties of neutral protease from B. subtilis have been investigated under a vari...
<p>Fluorescence emission of each protein collected at 0.20–0.33 mg/ml in 50 mM sodium phosphate, pH ...
The UV photodissociation kinetics of tryptophan amino acid, Trp, attached to the membrane of bacteri...
The decay of the tryptophanyl emission in proteins is often complex due to the sensitivity of the tr...
The decay of the tryptophanyl emission in proteins is often complex due to the sensitivity of the tr...
The intrinsic steady-state fluorescence and fluoresence decay of Staphylococcus epidermidis, Psuedom...
Time correlated single photon counting measurements of tryptophan (Trp) fluorescence intensity decay...
The picosecond time-resolved fluorescence decay of bacteriorhodopsin (BR) was analyzed by the maximu...
The fluorescence of the single tryptophan in Bacillus stearothermophilus phosphofructokinase was cha...
<p>Tryptophan fluorescence spectra of different samples (0.1 mg/ml protein) were recorded from 310–4...
AbstractA power-like decay function, characterized by the mean excited-state lifetime and relative v...
The fluorescence and phosphorescence spectra of model indole compounds and of cod parvalbumin III, a...
most probable spectral classes of emitting tryptophan residues and differences among the classes wer...
The time-resolved fluorescence properties of the bacteriophage T4 capsid protein gp23 are investigat...
Double-exponential decay has been observed for tryptophan and tryptophan-containing dipeptides. The ...
The fluorescence properties of neutral protease from B. subtilis have been investigated under a vari...
<p>Fluorescence emission of each protein collected at 0.20–0.33 mg/ml in 50 mM sodium phosphate, pH ...