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Proceedings Paper

Simulations on the kindling mechanism of the asFP595 fluorescent protein
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Paper Abstract

We report the results of quantum mechanical - molecular mechanical (QM/MM) simulations aiming to elucidate the mechanism of kindling of the initially non-fluorescent protein asFP595, which is a mutated variant of the chromoprotein asCP from the sea anemone Anemonia sulcata. asFP595 becomes brightly fluorescent (kindles) with emission at 595 nm in response to intense light irradiation at 568 nm. In simulations, we use the flexible effective fragment QM/MM method with the complete active space self-consistent field (CASSCF) wavefunctions in the quantum part and the AMBER force field parameters in the molecular mechanical part. We analyze the computed scans over potential energy surfaces of the ground and excited electronic states and consider details of the working hypothesis that the trans-cis isomerization of the chromophore group inside the protein is responsible for kindling.

Paper Details

Date Published: 13 February 2008
PDF: 6 pages
Proc. SPIE 6868, Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes, 686805 (13 February 2008); doi: 10.1117/12.760963
Show Author Affiliations
Bella L. Grigorenko, M.V. Lomonosov Moscow State Univ. (Russia)
Alexander V. Nemukhin, M.V. Lomonosov Moscow State Univ. (Russia)
N.M. Emanuel Institute of Biochemical Physics (Russia)
Alexander P. Savitsky, A.N. Bach Institute of Biochemistry (Russia)

Published in SPIE Proceedings Vol. 6868:
Small Animal Whole-Body Optical Imaging Based on Genetically Engineered Probes
Alexander P. Savitsky; Robert E. Campbell; Robert M. Hoffman, Editor(s)

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