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- W2085602665 startingPage "2971" @default.
- W2085602665 abstract "The emitting states of green fluorescent protein (GFP), monomeric Kusabira orange (mKO), and Discosoma red (DsRed) were studied using QM/MM and SAC-CI methods. By comparing the electronic structures among the green-, orange-, and red-emitting states as well as their electrostatic and quantum mechanical interactions within the protein cavity, the basic mechanisms for determining emission colors have been clarified. We found that the orange and red emissions of mKO and DsRed, respectively, result from cancellation between two effects, the pi skeleton extension (red shift) and protein electrostatic potential (blue shift). The extension of the pi skeleton enhances the intramolecular charge-transfer character of the transition, which makes the fluorescence energy more sensitive to the protein's electrostatic potential. On the basis of this mechanism, we predicted amino acid mutations that could red shift the emission energy of DsRed. A novel single amino acid mutation, which was examined computationally, reduced the DsRed emission energy from 2.14 (579 nm) to 1.95 eV (636 nm), which is approaching near-infrared fluorescence." @default.
- W2085602665 created "2016-06-24" @default.
- W2085602665 creator A5002853251 @default.
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- W2085602665 date "2010-02-04" @default.
- W2085602665 modified "2023-09-23" @default.
- W2085602665 title "Excited States of Fluorescent Proteins, mKO and DsRed: Chromophore−Protein Electrostatic Interaction Behind the Color Variations" @default.
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- W2085602665 doi "https://doi.org/10.1021/jp9099573" @default.
- W2085602665 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20131896" @default.
- W2085602665 hasPublicationYear "2010" @default.
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