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Comparison List

Monomeric hyperfolder YFP

a.k.a. mhYFP

Monomeric hyperfolder YFP is a basic (constitutively fluorescent) yellow fluorescent protein published in 2022, derived from Aequorea victoria. It is reported to be a rapidly-maturing monomer with moderate acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Aequorea victoria 27.0 kDa -

FPbase ID: PF2S1

Attributes

Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
515 529 124,000 0.62 76.88 5.7 27.0  

Photostability

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Monomeric hyperfolder YFP Sequence

Monomeric hyperfolder YFP was derived from Hyperfolder YFP with the following mutations: S147P/L195M/V206K
amino acid numbers relative to avGFP. show relative to Hyperfolder YFP

MVSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKLISTTGKLPVPWPTLVTTLGYGLMVFARYPDHMKQHDFFKSAMPEGYVQERTISFEDDGYYKTRAEVKFEGDTLVNRIVLKGIDFKEDGNILGHKLEYNFNPHNVYITADKQKNGIKANFKIRHNVEDGGVQLADHYQQNTPIGDGPVLMPDNHYLSYQSKLSKDPNEKRDHMVLKERVTAAGITHDMNELYK
GenBank: OP373687

Structure

Deposited: ,
Chromophore:

Excerpts

Introducing the S147P mutation that was reported to improve thermostability in violet-light excitable uvGFP yielded hyperfolder mutants with considerable resistance to 1 M sodium hydroxide (NaOH) solutions of pH ≥ 13 (we were able to determine hyperfolder FP extinction coefficients by collecting alkaline denaturation time-course data) (Extended Data Fig. 5 and Supplementary Methods). hfYFP-S147P/V206K/L195M behaved as a stronger monomer in the OSER assay than did hfYFP (Extended Data Fig. 3d,e); the L195M mutation originated de novo from a PCR error. The V206K mutation (on β-strand 10) largely preserved the GdnHCl stability of multiple mutants (Extended Data Fig. 4d). We named the hfYFP-S147P/V206K/L195M variant ‘mhYFP’.

Campbell et al. (2022)

Primary Reference

Additional References

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