Excited-state intramolecular proton transfer as a fluorescence probe for protein binding-site static polarity.

@article{Sytnik1994ExcitedstateIP,
  title={Excited-state intramolecular proton transfer as a fluorescence probe for protein binding-site static polarity.},
  author={A. Sytnik and M. Kasha},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 18},
  pages={
          8627-30
        }
}
  • A. Sytnik, M. Kasha
  • Published 1994
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
A fluorescence probe is introduced for protein conformation and binding-site monitoring as the proton-transfer (PT) tautomer fluorescence by using 4-hydroxy-5-azaphenanthrene (HAP) as a prototype. A typical grossly-wavelength-shifted PT fluorescence for HAP is observed in the 600-nm spectral region for this UV-absorbing molecule (absorption onset, 400 nm), for which case PT occurs even in protic solvents. It is shown that PT fluorescence of HAP can serve as a protein-binding-site static… Expand
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Solvents and Solvent Effects in Organic Chemistry
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