Fluorescence resonance energy transfer

Fluorescence resonance energy transfer (FRET) is the transfer of energy between two fluorophores, and is used to detect the interaction of two labelled molecules in close proximity. Single-molecule FRET methods are also used for molecular conformational studies.

Latest Research and Reviews

  • Protocols |

    This protocol describes fit-free analysis of fluorescence lifetime imaging microscopy (FLIM) data using the phasor approach. Pixel-by-pixel decays are transformed to the phasor space, and then the clusters can be connected to the image by the reciprocity rules of the phasor plots.

    • Suman Ranjit
    • , Leonel Malacrida
    • , David M. Jameson
    •  & Enrico Gratton
    Nature Protocols 13, 1979-2004
  • Research | | open

    A multi-laboratory study finds that single-molecule FRET is a reproducible and reliable approach for determining accurate distances in dye-labeled DNA duplexes.

    • Björn Hellenkamp
    • , Sonja Schmid
    • , Olga Doroshenko
    • , Oleg Opanasyuk
    • , Ralf Kühnemuth
    • , Soheila Rezaei Adariani
    • , Benjamin Ambrose
    • , Mikayel Aznauryan
    • , Anders Barth
    • , Victoria Birkedal
    • , Mark E. Bowen
    • , Hongtao Chen
    • , Thorben Cordes
    • , Tobias Eilert
    • , Carel Fijen
    • , Christian Gebhardt
    • , Markus Götz
    • , Giorgos Gouridis
    • , Enrico Gratton
    • , Taekjip Ha
    • , Pengyu Hao
    • , Christian A. Hanke
    • , Andreas Hartmann
    • , Jelle Hendrix
    • , Lasse L. Hildebrandt
    • , Verena Hirschfeld
    • , Johannes Hohlbein
    • , Boyang Hua
    • , Christian G. Hübner
    • , Eleni Kallis
    • , Achillefs N. Kapanidis
    • , Jae-Yeol Kim
    • , Georg Krainer
    • , Don C. Lamb
    • , Nam Ki Lee
    • , Edward A. Lemke
    • , Brié Levesque
    • , Marcia Levitus
    • , James J. McCann
    • , Nikolaus Naredi-Rainer
    • , Daniel Nettels
    • , Thuy Ngo
    • , Ruoyi Qiu
    • , Nicole C. Robb
    • , Carlheinz Röcker
    • , Hugo Sanabria
    • , Michael Schlierf
    • , Tim Schröder
    • , Benjamin Schuler
    • , Henning Seidel
    • , Lisa Streit
    • , Johann Thurn
    • , Philip Tinnefeld
    • , Swati Tyagi
    • , Niels Vandenberk
    • , Andrés Manuel Vera
    • , Keith R. Weninger
    • , Bettina Wünsch
    • , Inna S. Yanez-Orozco
    • , Jens Michaelis
    • , Claus A. M. Seidel
    • , Timothy D. Craggs
    •  & Thorsten Hugel
    Nature Methods 15, 669-676
  • Research | | open

    Hannes Schihada et al. report the design of 11 BRET-based biosensors that allow for quantification of GPCR ligand-binding dynamics in a micro-titer format. The biosensors achieve higher dynamic range and sensitivity than FRET-based biosensors and their design can be extended to the study of other receptor types.

    • Hannes Schihada
    • , Sylvie Vandenabeele
    • , Ulrike Zabel
    • , Monika Frank
    • , Martin J. Lohse
    •  & Isabella Maiellaro
  • Research | | open

    Louis-Philippe Picard et al. present a BRET-based biosensor for monitoring ligand- and transducer-mediated conformational changes in GPCRs. They apply the biosensor to β2AR, a prototypical class A GPCR, and demonstrate the ability of the biosensor to be multiplexed with other BRET-based biosensors.

    • Louis-Philippe Picard
    • , Anne Marie Schönegge
    • , Martin J. Lohse
    •  & Michel Bouvier

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