Fluorescence Molecular Relaxation Spectroscopy

Abstract

Fluorescence spectroscopy is a popular technique due to the simplicity of the experiments and high sensitivity of the parameters, which are determined, to structural changes in proteins. However, this method has not yet been developed to the extent of enabling a strict and unequivocal interpretation of protein structure, based on the spectra under study. Despite great research effort and an enormous amount of accumulated experimental data, we still have no definitive answers to the questions which faced investigators at the very beginning of the development of this method: What are the causes of spectral changes? What is the explanation for the large variation (up to 40 nm) exhibited by fluorescence spectra in proteins? To what extent is the approach based on the analysis of models of indole and tryptophan environment in isotropic media justified?