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The renaissance of fluorescence resonance energy transfer

Nature Structural Biology volume 7, pages 730–734 (2000)Cite this article

Abstract

Recent advances in fluorescence resonance energy transfer have led to qualitative and quantitative improvements in the technique, including increased spatial resolution, distance range, and sensitivity. These advances, due largely to new fluorescent dyes, but also to new optical methods and instrumentation, have opened up new biological applications.

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Figure 1: GFP based FRET was used to measure conformational changes in myosin upon ATP binding and hydrolysis.
Figure 2: FRET constructs for measuring intracellular calcium.
Figure 3: Conformational changes in a cysteine-light GFP-tagged kinesin.
Figure 4: Lanthanide-based resonance energy transfer.
Figure 5: Structure and lanthanide-based resonance energy transfer measurements of a voltage-controlled ion channel.
Figure 6: Fluorescence lifetime imaging FRET can be used to localize the position of phosphorylated biomolecules in a cell.

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Acknowledgements

This work was supported by the NIH.

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Authors and Affiliations

  1. Loomis Lab of Physics, University of Illinois, 1110 W. Green St, Urbana, 61801, Illinois, USA

    Paul R. Selvin

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  1. Paul R. Selvin
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Correspondence to Paul R. Selvin.

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Selvin, P. The renaissance of fluorescence resonance energy transfer. Nat Struct Mol Biol 7, 730–734 (2000). https://doi.org/10.1038/78948

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