Division of Tyrosine and Tryptophan Fluorescence Components

Abstract

The fluorescence of tryptophan and tyrosine residues is widely used in studies of the structure and dynamics of proteins [18, 22, 25, 67, 161]. Dividing of the tyrosine component from tryptophan component in the fluorescence spectrum of a protein and searching for individual bands of identical aromatic residues located in different microenvironments are an important task, especially in quantitative measurements of the efficiency of energy transfer [60, 162]. The tyrosine and tryptophan components are usually divided using two or three different excitation or emission wavelengths [67, 163]. For example, excitation of tryptophan residues is accomplished in the wavelength range of 285–300 nm, and excitation of tyrosine residues is accomplished at 275 nm [164].