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Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins

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Krapivin V. B., Stepanyuk R. A., Khrenova M. G. Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins // Mendeleev Communications. 2026. Vol. 36. No. 2. pp. 142-144.
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Krapivin V. B., Stepanyuk R. A., Khrenova M. G. Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins // Mendeleev Communications. 2026. Vol. 36. No. 2. pp. 142-144.
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TY - JOUR
DO - 10.71267/mencom.7869
UR - https://mendcomm.colab.ws/publications/10.71267/mencom.7869
TI - Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins
T2 - Mendeleev Communications
AU - Krapivin, Vladimir Borisovich
AU - Stepanyuk, Roman Alekseevich
AU - Khrenova, Mariya Grigor'evna
PY - 2026
DA - 2026/02/03
PB - Mendeleev Communications
SP - 142-144
IS - 2
VL - 36
ER -
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@article{2026_Krapivin,
author = {Vladimir Borisovich Krapivin and Roman Alekseevich Stepanyuk and Mariya Grigor'evna Khrenova},
title = {Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins},
journal = {Mendeleev Communications},
year = {2026},
volume = {36},
publisher = {Mendeleev Communications},
month = {Feb},
url = {https://mendcomm.colab.ws/publications/10.71267/mencom.7869},
number = {2},
pages = {142--144},
doi = {10.71267/mencom.7869}
}
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Krapivin, Vladimir Borisovich, et al. “Efficiency of green-to-red chromophore conversion for AzamiGreen-derived fluorescent proteins.” Mendeleev Communications, vol. 36, no. 2, Feb. 2026, pp. 142-144. https://mendcomm.colab.ws/publications/10.71267/mencom.7869.
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Keywords

chromophore resonance forms
ellipticity of electron density
green fluorescent proteins
natural resonance theory
quantum chemical calculations
red fluorescent proteins

Abstract

QM/MM calculations were performed to determine the energy differences between the green and red states of AzamiGreen fluorescent protein variants. The contributions of the resonance P- and I-forms of the chromophore were analyzed for a series of five proteins. A relationship was demonstrated between the contribution of the phenolate anionic form and the stabilization of the red state of the chromophore.

Funders

Russian Science Foundation
19-73-20032

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