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mTurquoise2

mTurquoise2 is a basic (constitutively fluorescent) cyan fluorescent protein published in 2012, derived from Aequorea victoria. It has very low acid sensitivity.
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Aggregation Organism Molecular Weight Cofactor
Monomer Aequorea victoria 26.9 kDa -

Attributes

Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
434 474 30,000 0.93 27.9 3.1   4.0

OSER Measurements

% Normal Cells OSER/NE ratio Cell Type Reference
93.8 ± 1.0 (10000 cells) - HeLa Cranfill et al. (2016)

Photostability

t1/2 (s) Power Light Mode In Cell Fusion ˚C Reference
90.0 Goedhart et al. (2012)

mTurquoise2 Sequence

mTurquoise2 was derived from mTurquoise with the following mutations: I146F
amino acid numbers relative to avGFP. show relative to mTurquoise

MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLSWGVQCFARYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYFSDNVYITADKQKNGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMVLLEFVTAAGITLGMDELYK

Structure

Deposited: ,
Chromophore:

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)

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folding characteristics in either bacteria or mammalian cells, while the spectral properties were unchanged (Goedhart, unpublished observation).

Primary Reference

Additional References

External Resources

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