Protein flexibility as revealed by fluorescence resonance energy transfer: An extension of the method for systems with multiple labels

Béla Somogyi, Zsuzsa Lakos, Ágnes Szarka, Miklós Nyitrai

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13 Citations (Scopus)


The temperature profile of the normalized fluorescence resonance energy transfer efficiency is capable of monitoring the relative change of flexibility and/or conformational state of macromolecules [Biochemistry 23 (1984) 3403]. The method described earlier for one donor-one acceptor systems is extended to multiple fluorophore systems when the energy transfer occurs between either one donor-m acceptors, or n donors-one acceptor or n donors-m acceptors (where n and m are integer values). It is shown that the normalized energy transfer efficiency obtained for systems containing multiple labels is a linear combination of the normalized transfer efficiency assigned to individual donor-acceptor pairs of the system, thus its temperature profile is capable of monitoring the change of intramolecular flexibility and/or conformational state.

Original languageEnglish
Pages (from-to)26-32
Number of pages7
JournalJournal of Photochemistry and Photobiology B: Biology
Issue number1-3
Publication statusPublished - Jan 1 2000



  • Fluorescence resonance energy transfer
  • Protein flexibility

ASJC Scopus subject areas

  • Radiation
  • Radiological and Ultrasound Technology
  • Biophysics
  • Radiology Nuclear Medicine and imaging

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