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Issue 16, 2012
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A combined quantum mechanics/molecular mechanics study of the one- and two-photon absorption in the green fluorescent protein

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Abstract

We present for the first time a QM/MM study of the one- and two-photon absorption spectra of the GFP chromophore embedded in the full protein environment described by an advanced quantum mechanically derived polarizable force field. The calculations are performed on a crystal structure of the green fluorescent protein (GFP) using the polarizable embedding density functional theory (PE-DFT) scheme. The importance of treating the protein environment explicitly with a polarizable force field and higher-order multipoles is demonstrated, as well as the importance of including water molecules close to the chromophore in the protein barrel. For the most advanced description we achieve good agreement with experimental findings, with a peak at 405 nm for the neutral and a peak at 475 nm for the anionic form of the GFP chromophore. The presence of a dark OPA state, as suggested by other studies to explain the discrepancies between OPA and TPA spectra, is not supported by our calculations.

Graphical abstract: A combined quantum mechanics/molecular mechanics study of the one- and two-photon absorption in the green fluorescent protein

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Publication details

The article was received on 10 Nov 2011, accepted on 25 Jan 2012 and first published on 01 Feb 2012


Article type: Paper
DOI: 10.1039/C2CP23537D
Citation: Phys. Chem. Chem. Phys., 2012,14, 5440-5451
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    A combined quantum mechanics/molecular mechanics study of the one- and two-photon absorption in the green fluorescent protein

    A. H. Steindal, J. M. H. Olsen, K. Ruud, L. Frediani and J. Kongsted, Phys. Chem. Chem. Phys., 2012, 14, 5440
    DOI: 10.1039/C2CP23537D

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