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Protein Fluorescence

  • Joseph R. Lakowicz

Abstract

Discussions of biochemical fluorescence frequently start with the subject of protein fluorescence. This is because, among biopolymers, proteins are unique in displaying useful intrinsic fluorescence. Lipids, membranes, and saccharides are essentially nonfluorescent, and the intrinsic fluorescence of DNA is too weak to be useful. In proteins, the three aromatic amino acids—phenylalanine, tyrosine, and tryptophan—are all fluorescent. A favorable feature of protein structure is that these three amino acids are relatively rare in proteins. Tryptophan, which is the dominant intrinsic fluorophore, is generally present at about 1 mol % in proteins. A protein may possess just one or a few tryptophan residues, which facilitates interpretation of the spectral data. If all 20 amino acids were fluorescent, it is probable that protein emission would be too complex to interpret.

Keywords

Emission Spectrum Tryptophan Residue Tryptophan Fluorescence Relative Quantum Yield Staphylococcal Nuclease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1999

Authors and Affiliations

  • Joseph R. Lakowicz
    • 1
  1. 1.University of Maryland School of MedicineBaltimoreUSA

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