Theory of bio-energy transport in protein molecules and its experimental evidences as well as applications (I)

Chen

Wang

et al. 2016

IJMS

The influences of electromagnetic fields (EMFs) on bio-energy transport and its mechanism of changes are investigated through analytic and numerical simulation and experimentation. Bio-energy transport along protein molecules is performed by soliton movement caused by the dipole–dipole electric interactions between neighboring amino acid residues. As such, EMFs can affect the structure of protein molecules and change the properties of the bio-energy transported in living systems. This mechanism of biological effect from EMFs involves the amino acid residues in protein molecules. To study and reveal this mechanism, we simulated numerically the features of the movement of solitons along protein molecules with both a single chain and with three channels by using the Runge–Kutta method and Pang’s soliton model under the action of EMFs with the strengths of 25,500, 51,000, 76,500, and 102,000 V/m in the single-chain protein, as well as 17,000, 25,500, and 34,000 V/m in the three-chain protein, respectively. Results indicate that electric fields (EFs) depress the binding energy of the soliton, decrease its amplitude, and change its wave form. Also, the soliton disperses at 102,000 V/m in a single-chain protein and at 25,500 and 34,000 V/m in three-chain proteins. These findings signify that the influence of EMFs on the bio-energy transport cannot be neglected; however, these variations depend on both the strength and the direction of the EF in the EMF. This direction influences the biological effects of EMF, which decrease with increases in the angle between the direction of the EF and that of the dipole moment of amino acid residues; however, randomness at the macroscopic level remains. Lastly, we experimentally confirm the existence of a soliton and the validity of our conclusion by using the infrared spectra of absorption of the collagens, which is activated by another type of EF. Thus, we can affirm that both the described mechanism and the corresponding theory are correct and that EMFs or EFs can influence the features of energy transport in living systems and thus have certain biological effects.

Section: Theories Of Energy Transport In Protein Molecules and Thementioning

confidence: 99%

Influences of Electromagnetic Energy on Bio-Energy Transport through Protein Molecules in Living Systems and Its Experimental Evidence

Chen

Wang

et al. 2016

IJMS

“…This is just the Davydov model for bio-energy transport which he first proposed in α-helix protein molecules in Fig. 1 in the 1970s [1]. Davydov's idea yields a compelling picture of the mechanism of bio-energy transport in protein molecules and consequently has been the subject of a large number of work [2 − 16].…”

Section: ½ áòøöó ù ø óòmentioning

confidence: 99%

“…Usually for all parameters in Eqs. (1) and (2) site-independent mean values are used. The average value of the dipoledipole coupling between neighboring amide-I oscillators is J=0.967 meV.…”

Section: ½ áòøöó ù ø óòmentioning

confidence: 99%

Influence of structure disorders and temperatures of systems on the bio-energy transport in protein molecules (II)

2008

Front. Phys. China

Self Cite

The influence of molecular structure disorders and physiological temperature on the states and properties of solitons as transporters of bio-energy are numerically studied through the fourth-order RungeKutta method and a new theory based on my paper [Front. Phys. China, 2007, 2(4): 469]. The structure disorders include fluctuations in the characteristic parameters of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the chain-chain interaction coefficient among the three channels and ground state energy resulting from the disorder distributions of masses of amino acid residues and impurities. In this paper, we investigate the behaviors and states of solitons in a single protein molecular chain, and in α-Helix protein molecules with three channels. In the former we prove first that the new solitons can move without dispersion, retaining its shape, velocity and energy in a uniform and periodic protein molecule. In this case of structure disorder, the fluctuations of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the ground state energy and the disorder distributions of masses of amino acid residues of the proteins influence the states and properties of motion of solitons. However, they are still quite stable and are very robust against these structure disorders, even in the presence of larger disorders in the sequence of masses, spring constants and coupling constants. Still, the solitons may disperse or be destroyed when the disorder distribution of the masses and fluctuations of structure parameters are quite great. If the effect of thermal perturbation of the environment on the soliton in nonuniform proteins is considered again, it is still thermally stable at the biological temperature of 300 K, and at the longer time period of 300 ps and larger spacing of 400 amino acids. The new soliton is also thermally stable in the case of motion over a long time period of 300 ps in the region of 300− 320 K under the influence of the above structure disorders. However, the soliton disperses in the case of a higher temperature of 325 K and in larger structure disorders. Thus, we determine that the soliton's lifetime and critical temperature are 300 ps and 300−320 K, respectively. These results are also consistent with analytical data obtained via quantum perturbed theory. In α-helix protein molecules with three channels, results obtained show that these structure disorders and quantum fluctuations can change the states and features of solitons, decrease their amplitudes, energies and velocities, but they still cannot destroy the solitons, which can still transport steadily along the molecular chains while retaining energy and momentum when the quantum fluctuations are small, such as in structure disorders and quantum fluctuations of 0.67 < α k < 2, ΔW = ±8%W , ΔJ = ±1%J, Δ(χ 1 + χ 2 ) = ±3%(χ 1 + χ 2 ) and ΔL = ±1%L and Δε 0 = ε|β n |, ε=0.1 meV, |β n | < 0.5. Therefore, the solitons in the improved model are qui...

“…Therefore, it is quite necessary to further study the influence of structural non-uniformity on Pang's soliton in the region of 300-310 K using the above method. [71][72][73][74][75][76][77][78][79][80][81][82] The behavior of Pang's soliton is shown in Fig. 44, when the disorder of the mass sequence is in the region of 0.67M < M k < 2M , where ∆J = ±5% J, ∆(χ 1 + χ 2 ) = ±5% (χ 1 + χ 2 ), ∆w = ±10% w, |β| ≤ 0.5, for T = 300 K, T = 310 K, T = 315 K and T = 320 K, respectively.…”

Section: The Results In Single Chain Protein In Pang's Modelmentioning

confidence: 99%

“…Therefore, we can conclude that Pang's soliton is robust against thermal perturbation and structural non-uniformity of the α-helical protein molecules at biological temperatures. Thus, the soliton in Pang's model [71][72][73][74][75][76][77][78][79][80][81][82] is an exact carrier for bio-energy transport in the α-helical protein molecules with three channels. In Fig.…”

Section: The Results In α-Helical Protein Molecules With Three Channementioning

confidence: 99%

The Checkout and Verification of Theory of Bio-Energy Transport in the Protein Molecules

2014

Biophys. Rev. Lett.

The phosphorylation and de-phosphorylation reactions in the cell, through which the bio-energy is released from ATP hydrolysis in biological systems, are described in this paper. Firstly, the bio-energy is accepted by the vibrational amides in protein molecules in virtue of resonant mechanism of frequency or energy, and can transport along the protein molecules in soliton, which is formed by self-trapping of vibrational quantum (or exciton), by means of dipole-dipole interaction among the neighboring peptide groups (or amino acids). Theory and properties of bio-energy transport were proposed and described by many researchers. We here reviewed mainly the theories and features of Davydov's and Pang's models. However these theoretical models including Davydov's and Pang's model were all established based on a periodic and uniform proteins, which are different from practically biological proteins molecules. Therefore, it is necessary to inspect and verify the validity of the theory of bio-energy transport in real biological protein molecules. These problems were extensively studied by a lot of researchers using different methods in past thirty years, a considerable number of research results were obtained. I review here the situation and progresses of study on this problem, in which we reviewed the correctness of the theory of bio-energy transport including Davydov's and Pang's model and its investigated progresses under influences of structural nonuniformity and disorder, side groups and imported impurities of protein chains as well as the thermal perturbation and damping of medium arising from the biological temperature of the systems. The structural non-uniformity arises from the disorder distribution of sequence of masses of amino acid residues, side groups and imported impurities, which results in the changes and fluctuations of the spring constant, dipole-dipole interaction, exciton-phonon coupling constant, diagonal disorder or ground state energy and chainchain interaction of the molecular channels in the dynamic equations in different models. The influences of structural non-uniformity, side groups and imported impurities as well as the thermal perturbation and damping of medium on the bio-energy transport in the proteins with single chain and three chains were studied by different numerical simulation techniques and methods including the average Hamiltonian way of thermal 1 Biophys. Rev. Lett. 2014.09:1-79. Downloaded from www.worldscientific.com by KING MONGKUT'S UNIVERSITY OF TECHNOLOGY THONBURI on 10/14/14. For personal use only. 2 X.-F. Pangperturbation, fourth-order Runge-Kutta method, Monte Carlo method, quantum perturbed way and thermodynamic and statistical method, and so on. In this review, the numerical simulation results of bio-energy transport in uniform protein molecules, the influence of structural non-uniformity on the bio-energy transport, the effects of system temperature on the bio-energy transport and the simultaneous effects of structural nonuniformity, damping and thermal perturbation o...