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- W2024806163 abstract "Fluorescent proteins are important reporter molecules widely used in biotechnology and the biological sciences, generally. Their unusual spectrophotometric and fluorescence characteristics are controlled via protonation states of the chromophore, as for green fluorescent proteins (GFPs), and/or via cis–trans isomerization of the chromophore, as for red fluorescent proteins (RFPs). Here, we have performed both quantum mechanical calculations on substituted chromophores and structural comparisons of several RFPs (Rtms5, eqFP611, HcRed, and DsRed) and wild-type GFP. Our results indicate that the chromophore cis and trans isomers are comparably stable, and cis–trans isomerization has only a minor effect on electronic excitation. The chromophore is also found to exist in either the anionic or possibly zwitterionic protonation state. Structural comparisons of RFPs reveal that the conformation of the chromophore within a specific RFP is determined by only a few key residues, which could serve as mutation targets for engineering new fluorescent proteins for novel biotechnological applications." @default.
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- W2024806163 date "2009-12-01" @default.
- W2024806163 modified "2023-09-23" @default.
- W2024806163 title "PROTONATION STATES AND CONFORMATIONAL FLEXIBILITY OF THE RED FLUORESCENT PROTEIN CHROMOPHORE" @default.
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- W2024806163 doi "https://doi.org/10.1142/s0219633609005362" @default.
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