a.k.a. mhYFP
| Oligomerization | Organism | Molecular Weight | Cofactor |
|---|---|---|---|
| Monomer | Aequorea victoria | 27.0 kDa | - |
| 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 |
No photostability measurements available ... add one!
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
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)
(2022). Nature Methods, , . doi: 10.1038/s41592-022-01660-7. Article Pubmed
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