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. Author manuscript; available in PMC: 2009 Oct 20.
Published in final edited form as: Chem Biol. 2008 Oct 20;15(10):1116–1124. doi: 10.1016/j.chembiol.2008.08.006

Table 3.

FRET characteristics for several fusion constructs of the fluorescent proteins.

Fusion construct Förster distance, R0, nm FRET efficiency, E Reference
mTagBFP-mTagGFP 5.25 0.57 ± 0.03 this paper
EBFP2-mTagGFP 5.13 0.38 ± 0.03 this paper
ECFP-EYFP * 4.86 0.42 *** [24, 31]
mCyPet-mYPet ** 4.93 **** 0.51 *** [32, 33]

Förster distances were calculated under the standard assumption of the random orientation of the chromophores. FRET efficiencies were experimentally measured using the physically linked donor and acceptor proteins.

*

Proteins of this widely used standard FRET pair have a tendency to form a dimer. Data on monomerized versions of the proteins are not available.

**

Monomerized versions of CyPet and YPet proteins, which have been specifically optimized for FRET through multiple rounds of site-specific and random mutagenesis [33]. It has been recently shown though that the original CyPet and YPet proteins form hetero- and homo-dimers in solution that substantially enhanced the observed FRET efficiency [33].

***

ECFP-EYFP pair has 9-amino acid linker [24]. mCyPet-mYPet pair has 12-amino acid linker [33].

*****

Calculated from the data [32].