Tryptophan octyl ester in detergent micelles of dodecylmaltoside: fluorescence properties and quenching by brominated detergent analogs.

@article{Foresta1999TryptophanOE,
  title={Tryptophan octyl ester in detergent micelles of dodecylmaltoside: fluorescence properties and quenching by brominated detergent analogs.},
  author={B{\'e}atrice de Foresta and Jacques Gallay and Jana Sopkov{\'a} and Philippe Champeil and Myl{\`e}ne Vincent},
  journal={Biophysical journal},
  year={1999},
  volume={77 6},
  pages={
          3071-84
        }
}
The fluorescence properties of tryptophan octyl ester (TOE), a hydrophobic model of Trp in proteins, were investigated in various mixed micelles of dodecylmaltoside (DM) and 7,8-dibromododecyl beta-maltoside (BrDM) or 10,11-dibromoundecanoyl beta-maltoside (BrUM). This study focuses on the mechanism via which these brominated detergents quench the fluorescence of TOE in a micellar system. The experiments were performed at a pH at which TOE is uncharged and almost completely bound to detergent… CONTINUE READING
BETA

Similar Papers

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 14 CITATIONS