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Despite significant interest to the structures and spectra of fluorescent proteins plenty of details regarding their properties remain hidden, even considering the parent member of the family, the green fluorescent protein. We shall report results of recent QM/MM based simulations of structures on the ground and excited electronic states as well as optical spectra of GFP and related proteins. Those include calculations of the energy landscape along the assumed proton transfer route in GFP involving the conventional A, I, and B conformational forms with different protonation states of the chromophore. We characterize the computationally constructed GFP variants in which the anionic chromophore is sandwiched between two tyrosine residues in a triple-decker motif. Properties of the kindling fluorescent protein, the Ala143Gly variant of the natural chromoprotein asFP595, will be also considered.