Fluorescence Decay Studies of Peptide-Nucleic Acid Complexes

  • Thérèse Montenay-Garestier
  • Masashi Takasugi
  • Trung Le Doan
Conference paper
Part of the The Jerusalem Symposia on Quantum Chemistry and Biochemistry book series (JSQC, volume 16)

Abstract

Fluorescence decay studies of two tryptophan-containing peptides and one tyrosine-containing peptide reveal the existence of at least two conformers for each peptide. When these peptides bind to poly(U), denatured or native DNA changes are observed in both the lifetimes and the respective contributions of the two components. A model is proposed in which each peptide conformer forms two types of complexes, one involving only electrostatic interactions, the second one involving both electrostatic and stacking interactions. Moreover energy transfer from tyrosine to nucleic acid bases is shown to play an important role in the quenching of the fluorescence of tyrosine-containing peptides bound to nucleic acids.

Keywords

Fluorescence Lifetime Fluorescence Quantum Yield Fluorescence Decay Nucleic Acid Basis Exponential Decay Function 
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

© D. Reidel Publishing Company 1983

Authors and Affiliations

  • Thérèse Montenay-Garestier
    • 1
  • Masashi Takasugi
    • 1
  • Trung Le Doan
    • 1
  1. 1.Laboratoire de BiophysiqueINSERM U201, ERA CNRS 951, Muséum National d’Histoire NaturelleParisFrance

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