ArticleRSC advances2024
Modulating the pH dependent photophysical properties of green fluorescent protein.
Article in RSC advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Functional customization of peptide linkers in fusion proteins through multimodal deep learning approach.Synthetic and systems biotechnology · 2026Article
- 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
- Intensity-Based Estimation of Monomeric Brightness for Fluorescent Proteins.International journal of molecular sciences · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The photophysical properties of the β-barrel superfolder green fluorescent protein (sfGFP) arise from the chromophore that forms post-translationally in the interior of the protein. Specifically, the protonation state of the side chain of tyrosine 66 in the chromophore, in addition to the network of hydrogen bonds between the chromophore and surrounding residues, is directly related to the electronic absorbance and emission properties of the protein. The pH dependence of the photophysical properties of this protein were modulated by the genetic, site-specific incorporation of 3-nitro-l-tyrosine (mNO
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Registered trials
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