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Issue 13, 2013
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Electrostatic spectral tuning mechanism of the green fluorescent protein

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Abstract

Understanding the mechanism of spectral tuning of biological chromophores is a major challenge in photobiology. We show here using large-scale full quantum chemical calculations of the green fluorescent protein that state-of-the-art coupled-cluster calculations provide accurate excitation energies and detailed insight about specific environmental effects. We obtain vertical excitation energies of 3.13 eV (396 nm) and 2.68 eV (463 nm), which are in quantitative agreement with the experimental absorption energies of 3.12 eV (397 nm) and 2.61 eV (475 nm) for the A- and B-forms of the protein. We find that the protein environment redshifts the absorption spectra by ∼0.56 eV and ∼0.22 eV for the two states, which can be attributed to ∼80% electrostatic effects and ∼20% steric effects.

Graphical abstract: Electrostatic spectral tuning mechanism of the green fluorescent protein

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Publication details

The article was received on 07 Jan 2013, accepted on 04 Feb 2013 and first published on 11 Feb 2013


Article type: Communication
DOI: 10.1039/C3CP00058C
Citation: Phys. Chem. Chem. Phys., 2013,15, 4491-4495
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    Electrostatic spectral tuning mechanism of the green fluorescent protein

    V. R. I. Kaila, R. Send and D. Sundholm, Phys. Chem. Chem. Phys., 2013, 15, 4491
    DOI: 10.1039/C3CP00058C

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