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• W4312123590 endingPage "15640" @default.
• W4312123590 startingPage "15640" @default.
• W4312123590 abstract "Fluorescent Proteins are widely studied for their multiple applications in technological and biotechnological fields. Despite this, they continue to represent a challenge in terms of a complete understanding of all the non-equilibrium photo-induced processes that rule their properties. In this context, a theoretical-computational approach can support experimental results in unveiling and understanding the processes taking place after electronic excitation. A non-standard cyan fluorescent protein, psamFP488, is characterized by an absorption maximum that is blue-shifted in comparison to other cyan fluorescent proteins. This protein is characterized by an extended Stokes shift and an ultrafast (170 fs) excited state proton transfer. In this work, a theoretical-computational study, including excited state ab initio dynamics, is performed to help understanding the reaction mechanism and propose new hypotheses on the role of the residues surrounding the chromophore. Our results suggest that the proton transfer could be indirect toward the acceptor (Glu167) and involves other residues surrounding the chromophore, despite the ultrafast kinetics." @default.
• W4312123590 created "2023-01-04" @default.
• W4312123590 creator A5018498770 @default.
• W4312123590 creator A5082554755 @default.
• W4312123590 date "2022-12-09" @default.
• W4312123590 modified "2023-10-14" @default.
• W4312123590 title "Direct or Indirect ESPT Mechanism in CFP psamFP488? A Theoretical-Computational Investigation" @default.
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• W4312123590 doi "https://doi.org/10.3390/ijms232415640" @default.
• W4312123590 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36555282" @default.
• W4312123590 hasPublicationYear "2022" @default.
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