mTurquoise2

Excerpts

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.

Goedhart et al. (2012)

mTurquoise2 is an excellent fluorescent protein for imaging embryogenesis, allowing rapid and dynamic cellular processes (e.g. cleavage division) to be captured, while at the same time enabling long imaging sessions, with low photo-bleaching and limited photo toxicity.

DuBuc et al. (2014)

Thus, the stable and intense expression of mTurquoise2, either alone or in combination with other fluorescent reporters of infection in dual and triple infection experiments, does not appear to increase cytopathology of infected neurons

Hogue et al. (2018)

In mTurquoise2, the direction of the transition dipole moment is 4° from the line connecting the centers of the aromatic rings.

Myšková et al. (2020)

Expression of the cyan fluorescent proteins mTurquoise2 and mTFP*1 were easily differentiable from background fluorescence in wild-type (P < 0.001), with a quantitative comparison showing mTurquoise2 possessing the greatest relative intensity

Spencer et al. (2020)

Notably, when both mTurquoise2 and mNeonGreen donors were included simultaneously, double-labeled cells could be found, which appeared to be capable of dividing (Figure 4—figure supplement 1), indicating that FP labeling does not affect cell viability in diploid CRISPIEd cells

Zhong et al. (2021)

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folding characteristics in either bacteria or mammalian cells, while the spectral properties were unchanged (Goedhart, unpublished observation).

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