title: [Coherent singlet-triplet transitions at the initial step of tubulin assembly into microtubules].
abstract: Quantum chemistry calculations [DFT-B3LYP QM/MM method, 6-31G** basis set, + ab initio molecular dynamics] were used to study the action of Mg2+ on tubulin properties. It was shown that the hydration of the guanosine triphosphate-tubulin forms a protein zone structure, which includes a electron-occupied zone and a conductivity zone. The binding of Mg2+ to guanosine triphosphate-tubulin results in the unpairing of electrons in the occupied zone (triplet state formation) followed by their transition to the conductivity zone in which the inversion of spin occurs (singlet state formation). The formation of triplet state is the initial step in the subsequent protein dynamics in the picosecond range of time. The dynamics shows up as a coherent oscillating transition of tubulin between the triplet and singlet states, which is evidence of a simultaneous adjustment between nuclear and electron configurations of the protein (ab initio molecular dynamics calculations). The barrier between the triplet and singlet states does not exceed 0.60 kcal x mol(-1). The barrier overcome is considered as electron tunneling through the Fermi surface, which separates the occupied and conductivity zones. Zone formation occurs in the presence of the shell of biological water surrounding the protein.
authors.forename: A A
authors.initials: AA
authors.lastname: Tulub
mesh_terms: D008870:Microtubules / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D013816:Thermodynamics; D014404:Tubulin / Q000737:chemistry*
chemical_list: D014404:Tubulin