ArticleThe journal of physical chemistry. B2012
Describing two-photon absorptivity of fluorescent proteins with a new vibronic coupling mechanism.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Synthesis and Optical Properties of Unsymmetric Aromatically π-Extended BODIPY.The Journal of organic chemistry · 2025Article
- Bipartite Genetically Encoded Biosensors to Sense Calcium Ion Dynamics at Membrane-Membrane Contact Sites.Analytical chemistry · 2025Article
- Simulations of Two-Photon Absorption Spectra of Fluorescent Dyes: The Impact of Non-Condon Effects.Journal of chemical theory and computation · 2025Article
- Engineering the ChlorON Series: Turn-On Fluorescent Protein Sensors for Imaging Labile Chloride in Living Cells.ACS central science · 2024Article
- Structural and photophysical characterization of the small ultra-red fluorescent protein.Nature communications · 2023Article
- Impact of the Protein Environment on Two-Photon Absorption Cross-Sections of the GFP Chromophore Anion Resolved at the XMCQDPT2 Level of Theory.International journal of molecular sciences · 2023Article
- Unveiling a new aspect of oxocarbons: open-shell character of 4- and 5-membered oxocarbon derivatives showing near-infrared absorption.Chemical science · 2023Article
- Choosing Bad versus Worse: Predictions of Two-Photon-Absorption Strengths Based on Popular Density Functional Approximations.Journal of chemical theory and computation · 2022Article
- Local Electric Field Controls Fluorescence Quantum Yield of Red and Far-Red Fluorescent Proteins.Frontiers in molecular biosciences · 2021Article
- An ultrasensitive biosensor for high-resolution kinase activity imaging in awake mice.Nature chemical biology · 2021Article
- High throughput instrument to screen fluorescent proteins under two-photon excitation.Biomedical optics express · 2020Article
- Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins.Journal of the American Chemical Society · 2019Article
- Blue-Shifted Green Fluorescent Protein Homologues Are Brighter than Enhanced Green Fluorescent Protein under Two-Photon Excitation.The journal of physical chemistry letters · 2017Article
- Deciphering the molecular mechanism responsible for GCaMP6m's Ca2+-dependent change in fluorescence.PloS one · 2017Article
- Long- and Short-Range Electrostatic Fields in GFP Mutants: Implications for Spectral Tuning.Scientific reports · 2015Article
- Green fluorescent protein with anionic tryptophan-based chromophore and long fluorescence lifetime.Biophysical journal · 2015Article
- Two-photon directed evolution of green fluorescent proteins.Scientific reports · 2015Article
- Primary role of the chromophore bond length alternation in reversible photoconversion of red fluorescence proteins.Scientific reports · 2012Article
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Authors and funding
5 authors.
Funding
Abstract
Fluorescent proteins (FPs) are widely used in two-photon microscopy as genetically encoded probes. Understanding the physical basics of their two-photon absorption (2PA) properties is therefore crucial for creation of two-photon brighter mutants. On the other hand, it can give us better insight into molecular interactions of the FP chromophore with a complex protein environment. It is known that, compared to the one-photon absorption spectrum, where the pure electronic transition is the strongest, the 2PA spectrum of a number of FPs is dominated by a vibronic transition. The physical mechanism of such intensity redistribution is not understood. Here, we present a new physical model that explains this effect through the "Herzberg-Teller"-type vibronic coupling of the difference between the permanent dipole moments in the ground and excited states (Δμ) to the bond-length-alternating coordinate. This model also enables us to quantitatively describe a large variability of the 2PA peak intensity in a series of red FPs with the same chromophore through the interference between the "Herzberg-Teller" and Franck-Condon terms.
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