Abstract
In intrinsic tryptophan fluorescence spectra and in the spectra of fluorescence probes associated with proteins, the dependence of fluorescence spectra on excitation wavelength (at the long-wave excitation) and of the excitation spectra on the wavelength of emission are observed. Similar observations have been reported earlier in vitrified solutions of dyes. The model of this phenomenon is proposed, based on photoselection of chromophores with different interaction with the environment and delayed structural relaxation in the excited state. The results show that on the nanosecond timescale the structural relaxation of the environment of the excited chromophore is not complete. This suggests the new interpretation of various data on protein molecular interaction and enzyme catalytic processes.
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