Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs

@article{Visser2009TimeresolvedFF,
  title={Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs},
  author={Antonie J. W. G. Visser and Sergey P Laptenok and Nina V. Visser and A. E. M. van den Hoek and David J. S. Birch and J.-C. Brochon and Jan Willem Borst},
  journal={European Biophysics Journal},
  year={2009},
  volume={39},
  pages={241-253}
}
Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible fluorescent proteins (VFPs) are widely used as spectrally different FRET pairs, where one VFP acts as a donor and another VFP as an acceptor. The VFPs are usually fused to the proteins of interest, and this fusion product is genetically encoded in cells. FRET between VFPs can be determined by analysis of either the fluorescence decay properties of… CONTINUE READING