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Detection of Förster resonance energy transfer (FRET) between
cyan and yellow fluorescent proteins is a key method for quantifying
dynamic processes inside living cells. To compare the different cyan and
yellow fluorescent proteins, FRET efficiencies were measured for a set of
the possible donor:acceptor pairs. FRET between monomeric Cerulean and
Venus is more efficient than the ECFP:EYFP pair and has a 10% greater
Förster distance. We also compared several live cell microscopy
methods for measuring FRET. The greatest contrast for changes in
intramolecular FRET is obtained using a combination of ratiometric and
spectral imaging. However, this method is not appropriate for establishing
the presence of FRET without extra controls. Accurate FRET efficiencies
are obtained by fluorescence lifetime imaging microscopy, but these
measurements are difficult to collect and analyze. Acceptor photobleaching
is a common and simple method for measuring FRET efficiencies. However,
when applied to cyan to yellow fluorescent protein FRET, this method
becomes prone to an artifact that leads to overestimation of FRET
efficiency and false positive signals. FRET was also detected by measuring
the acceptor fluorescence anisotropy. Although difficult to quantify, this
method is exceptional for screening purposes, because it provides high
contrast for discriminating FRET.
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