Division of Tyrosine and Tryptophan Fluorescence Components

  • Nikolai L. Vekshin
Part of the Biological and Medical Physics Series book series (BIOMEDICAL)


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].


Tyrosine Residue Tryptophan Residue Wavelength Shift Tryptophan Fluorescence Synchronous Fluorescence 
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Copyright information

© Springer-Verlag Berlin Heidelberg 2002

Authors and Affiliations

  • Nikolai L. Vekshin
    • 1
  1. 1.Institute of Cell BiophysicsRussian Academy of ScienceMoscow Region, PushchinoRussia

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