|Ex λ||Em λ||EC (M-1 cm-1)||QY||Brightness||pKa||Maturation (min)||Lifetime (ns)|
|% Normal Cells||OSER/NE ratio||Cell Type||Reference|
|93.8 ± 1.0 (10000 cells)||-||HeLa||Cranfill et al. (2016)|
|88.0||-||-||Meiresonne et al. (2019)|
|t1/2 (s)||Power||Light||Mode||In Cell||Fusion||˚C||Reference|
|90.0||Goedhart et al. (2012)|
Structural analysis of mTurquoise unveiled one suboptimal residue, Ile146, which was targeted for further improvement... The X-ray structure of the the I146F mutant, dubbed mTurquoise2, reveals that the mutated residue contributes to an improved packing of the chromophore through many further van der Waals interactions. This increases the QY to 0.93, which is now the highest for a monomeric fluorescent protein.
In mTurquoise2, the direction of the transition dipole moment is 4° from the line connecting the centers of the aromatic rings.
Remarkably, introducing the super-folder GFP mutations (S30R, Y39N, N105T, and I171V) into mTurquoise2 yielded no apparent beneficial folding characteristics in either bacteria or mammalian cells, while the spectral properties were unchanged (Goedhart, unpublished observation).
(2017). , , . doi: 10.1101/160374. Article