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].
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© 2002 Springer-Verlag Berlin Heidelberg
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Vekshin, N.L. (2002). Division of Tyrosine and Tryptophan Fluorescence Components. In: Photonics of Biopolymers. Biological and Medical Physics Series. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-04947-1_7
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DOI: https://doi.org/10.1007/978-3-662-04947-1_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-07855-2
Online ISBN: 978-3-662-04947-1
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