Abstract

The importance of tryptophan-free proteins, such as the histones in chromatin or some regulatory proteins, becomes increasingly evident. Therefore, information on tyrosine fluorescence in peptides and proteins is required. Basic studies of symmetric tripeptides X-Tyr-X, with X = Gly, Ala, Leu, Val, Lys, reveal a considerable difference in D₂O effects, quenchability by ionic surface quenchers, fluorescence yield, and fluorescence decay curves, as measured with a conventional fluorescence spectrometer and a picosecond fluorescence decay spectrometer. The latter consists of a distributed feedback dye laser, which is pumped by an excimer laser and provides pulses of 15-ps FWHM and energy of 0.5 mJ. The decay curves are taken by a streak camera with a resolution of a few picoseconds.

© 1986 Optical Society of America