This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Time-resolved fluorescence spectroscopy of single tryptophan Cutinase protein revile unusual ultrafast decay of tryptophan excited state. We studied a pH and temperature effect on tryptophan fluorescence in order examine the effect of electrostatic interaction on the stabilization of tryptophan fluorescence. A fluorescence results are correlated with protein molecular modeling. We also study the kinetics of braking the disulfate bridge under UV light illuminati
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