ArticleActa crystallographica. Section D, Structural biology2021
Structural and spectrophotometric investigation of two unnatural amino-acid altered chromophores in the superfolder green fluorescent protein.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Superfolder Green Fluorescent Protein (sfGFP): A Versatile Tool for Biotechnology Research.Applied biochemistry and biotechnology · 2026Review
- Genetic Encoding of 3-Cyano-Tyrosine and Its Use in Controlling the Chromophore Isomeric State of the Fluorescent Protein mKate.International journal of molecular sciences · 2026Article
- Modulating the pH dependent photophysical properties of green fluorescent protein.RSC advances · 2024Article
- Expression and purification of fluorinated proteins from mammalian suspension culture.Methods in enzymology · 2024Article
- Directed Expression of Tracheal Antimicrobial Peptide as a Treatment for Bovine-AssociatedFrontiers in veterinary science · 2021Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The spectrophotometric properties of the green fluorescent protein (GFP) result from the post-translationally cyclized chromophore composed of three amino acids including a tyrosine at the center of the β-barrel protein. Altering the amino acids in the chromophore or the nearby region has resulted in numerous GFP variants with differing photophysical properties. To further examine the effect of small atomic changes in the chromophore on the structure and photophysical properties of GFP, the hydroxyl group of the chromophore tyrosine was replaced with a nitro or a cyano group. The structures and spectrophotometric properties of these superfolder GFP (sfGFP) variants with the unnatural amino acids (UAAs) 4-nitro-L-phenylalanine or 4-cyano-L-phenylalanine were explored. Notably, the characteristic 487 nm absorbance band of wild-type (wt) sfGFP is absent in both unnatural amino-acid-containing protein constructs (Tyr66pNO
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Registered trials
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