Probing protein-protein interactions with FRET-FLIM

C.A. Bücherl, J.C.M. Aker, S.C. de Vries, J.W. Borst

Research output: Chapter in Book/Report/Conference proceedingChapter

21 Citations (Scopus)


The quantification of molecular interactions or conformational changes can conveniently be studied by using Förster Resonance Energy Transfer (FRET) as a spectroscopic ruler. The FRET phenomenon describes the transfer of energy from a donor to an acceptor molecule, if they are in close proximity (
Original languageEnglish
Title of host publicationPlant Developmental Biology
EditorsL. Hennig, C. Köhler
Place of PublicationTotowa
PublisherHumana Press
ISBN (Electronic)9781607617655
ISBN (Print)9781607617648
Publication statusPublished - 2010

Publication series

NameMethods in molecular biology
PublisherSpringer Verlag
ISSN (Print)1064-3745

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  • Cite this

    Bücherl, C. A., Aker, J. C. M., de Vries, S. C., & Borst, J. W. (2010). Probing protein-protein interactions with FRET-FLIM. In L. Hennig, & C. Köhler (Eds.), Plant Developmental Biology (Vol. 655, pp. 389-399). (Methods in molecular biology). Totowa: Humana Press.