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mTurquoise2

mTurquoise2 is a basic (constitutively fluorescent) cyan fluorescent protein published in 2012, derived from Aequorea victoria. It is reported to be a rapidly-maturing monomer with very low acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Aequorea victoria 26.9 kDa -

FPbase ID: 7AV5G

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 33.5 4.0
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mTurquoise2 OSER Measurements

% 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)

Photostability

t1/2 (s) Power Light Mode In Cell Fusion ˚C Reference
90.0   Goedhart et al. (2012)
A caution on interpretation of photostability measurements
Add photostability info

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)

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)

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folding characteristics in either bacteria or mammalian cells, while the spectral properties were unchanged (Goedhart, unpublished observation).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

Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%

Goedhart J, Von Stetten D, Noirclerc-Savoye M, Lelimousin M, Joosen L, Hink Ma, Van Weeren L, Gadella Twj, Royant A

(2012). Nature Communications, 3(1) , 751. doi: 10.1038/ncomms1738. Article   Pubmed

Additional References

  1. Directionality of light absorption and emission in representative fluorescent proteins

    Myšková J, Rybakova O, Brynda J, Khoroshyy P, Bondar A, Lazar J

    (2020). Proceedings of the National Academy of Sciences, 117(51) , 32395-32401. doi: 10.1073/pnas.2017379117. Article   Pubmed

  2. Characterization of a spectrally diverse set of fluorescent proteins as FRET acceptors for mTurquoise2

    Mastop M, Bindels Ds, Shaner Nc, Postma M, Gadella Twj, Goedhart J

    (2017). Scientific Reports, 7(1) , 11999. doi: 10.1038/s41598-017-12212-x. Article   Pubmed

  3. Robust and Bright Genetically Encoded Fluorescent Markers for Highlighting Structures and Compartments in Mammalian Cells

    Chertkova Ao, Mastop M, Postma M, Van Bommel N, Van Der Niet S, Batenburg Kl, Joosen L, Gadella Twj, Okada Y, Goedhart J

    (2017). , , . doi: 10.1101/160374. Article

  4. Systematic characterization of maturation time of fluorescent proteins in living cells

    Balleza E, Kim Jm, Cluzel P

    (2017). Nature Methods, 15(1) , 47-51. doi: 10.1038/nmeth.4509. Article   Pubmed

  5. A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum

    Shaner Nc, Lambert Gg, Chammas A, Ni Y, Cranfill Pj, Baird Ma, Sell Br, Allen Jr, Day Rn, Israelsson M, Davidson Mw, Wang J

    (2013). Nature Methods, 10(5) , 407-409. doi: 10.1038/nmeth.2413. Article   Pubmed

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