Probing quantum coherence in a biological system by means of DNA amplification

Abstract

As a result of rapid decoherence, quantum effects in biological systems are usually confined to single electron or hydrogen delocalizations. In principle, molecular interactions at high temperatures can be guided by quantum coherence if embedded in a dynamics preventing decoherence. This was experimentally investigated by analyzing the thermodynamics, kinetics, and quantum mechanics of the primer/template duplex formation during DNA amplification by polymerase chain reaction. The structures of the two oligonucleotide primers used for amplification of a cDNA template were derived either from a repetitive motif or a fractal distribution of nucleotide residues. Contrary to the computer-based calculation of the primer melting temperatures ( T m) that predicted a higher T m for the non-fractal primer due to nearest-neighbor effects, it was found that the T m of the non-fractal primer was actually 2°C lower than that of its fractal counterpart. A thermodynamic analysis of the amplification reaction indicated that the primer annealing process followed Bose–Einstein instead of Boltzmann statistics, with an additional binding potential of μ=500 J/mol or 10 −21 J/molecule due to a superposition of binding states within the primer/template duplex. The temporal evolution of the Bose–Einstein state was determined by enzyme kinetic analysis of the association of the primer/template duplex to Taq polymerase. Assuming that collision with the enzyme interrupted the superposition, it was found that the Bose–Einstein state lasted for t dec=0.7×10 −12 s, corresponding to the energy dispersion (Δ E) of quantum coherent states ( μ=ΔE≥ h/ t dec). A quantum mechanical analysis revealed that the coherent state was stabilized by almost vanishing separation energies between distinct binding states during a temperature-driven shifting of the two DNA strands in the primer/template duplex. The additional binding potential is suggested to arise from a short-lived electron tunneling as the result of overlapping orbitals along the axis of the primer/template duplex. This effect was unique to the fractal primer due to the number of binding states that remained almost constant, irrespective of the size of shifting. It is suggested that fractal structures found in proteins or other macromolecules may facilitate a short-lived quantum coherent superposition of binding states. This may stabilize molecular complexes for rapid sorting of correct-from-false binding, e.g. during folding or association of macromolecules. The experimental model described in this paper provides a low-cost tool for simulating and probing quantum coherence in a biological system.