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. 2010 Mar 9;38(8):2645–2662. doi: 10.1093/nar/gkq152

Table 7.

FRET efficiencies for different combinations of interaction input and output devices

Protein pair
FRET method

Donor quenchinga

Acceptor emmissionb
Parallelc ±rap.d Parallelc ±rap.d
FKBP∼mCerulean Inline graphic FRB∼mCitrine 0.23 ± 0.010 0.21 ± 0.007 0.20 ± 0.004 0.19 ± 0.015
FRB∼mCerulean Inline graphic FKBP∼mCitrine 0.19 ± 0.004 0.18 ± 0.004 0.18 ± 0.002 0.17 ± 0.008
FKBP∼mCitrine Inline graphic FRB∼mCherry 0.28 ± 0.006 0.25 ± 0.003 0.10 ± 0.010 0.10 ± 0.012
FRB∼mCitrine Inline graphic FKBP∼mCherry 0.29 ± 0.008 0.25 ± 0.004 0.09 ± 0.022 0.12 ± 0.022
ZipInline graphic∼mCerulean Inline graphic ZipInline graphic∼mCitrine 0.001 ± 3e-5 0.060 ± 0.006
ZipInline graphic∼mCitrine Inline graphic ZipInline graphic∼mCherry 0.017 ± 4e-4 0.021 ± 0.015

aMeasuring quenching of donor fluorescence.

bMeasuring sensitized acceptor emission.

cComparing independent samples with and without donor (external control).

dComparing fluorescence before and after adding rapamycin (internal control).