This article deals with the proton migration in a tyrosine stack, which models the proton channels existing in a number of proteins, including tubulin. The magnesium ion Mg²⁺ within the complex with guanosine triphosphate facilitates dissociation of a water molecule through initiating a shift of protons along the chain composed of relatively distant tyrosine residues. The process is thermodynamically stable (ΔG₂₉₈ < 0). The energy barrier for the protein shift does not exceed 3.15 kJ/mole. A relatively weak electrostatic field mimicking electret properties of proteins facilitates long-distance proton migration.