Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching

A study presents a systematic examination of tryptophan fluorescence dynamics in proteins with femtosecond resolution, in which distinct patterns of femtosecond-resolved fluorescence transients from the blue to the red side of emission are characterized to distinguish local ultrafast salvation and electronic quenching. Tryptophan is found to be an ideal local optical probe for hydration dynamics and protein-water interactions as well as an excellent local molecular reporter for ultrafast electron transfer in proteins.