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IFP14ms.pdf (931.1 kB)

Modeling Structure and Absorption Spectra of the Bacteriophytochrome-Based Fluorescent Protein IFP1.4

submitted on 13.11.2019, 07:05 and posted on 29.11.2019, 19:10 by Igor Polyakov, Bella Grigorenko, Alexander Nemukhin

We report the results of quantum mechanics/molecular mechanics (QM/MM) simulations of structures and absorption spectra of the fluorescent protein IFP1.4 engineered from the chromophore-binding domain of Deinococcus radiodurans (DrCBD). In this work, we focus on different protonation states of the biliverdin chromophore in the red-absorbing form of the protein. To this goal, the protein with the all-protonated chromophore as well as the structures obtained by removal of protons from the biliverdin pyrrole rings to a suitable acceptor within the system are considered. Several quantum chemistry methods to compute the S0→S1 excitation energies are used in the QM part to estimate shifts in the absorption band maxima upon chromophore deprotonation.


Russian Science Foundation, 17-13-01051


Email Address of Submitting Author


Lomonosov Moscow State University



ORCID For Submitting Author


Declaration of Conflict of Interest

There is no conflict of interest

Version Notes

This is the first version of the manuscript