Investigation of the dynamics of the structure of biopolymers by the method of kinetic spectrofluorometry

A system for kinetic spectroscopy was developed and used to measure the kinetic characteristics of the intrinsic fluorescence of the dipeptide TRP–TRP and to separate the spectral-kinetic components corresponding to different indole chromophores of the dipeptide. The method of consecutive picosecond fluorescence probing of fast streams of liquid chemical reagents was used to detect changes in the average duration of the fluorescence of the intramolecular chromophores during a single elementary event of enzymic catalysis. New potential applications were found for the laser spectral-kinetic methods in a study of the dynamics of the structure of biological molecules under biochemical reaction and equilibrium conditions.