Abstract
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.
Highlights
Prevalent in our environment, electromagnetic fields (EMFs) or waves (EMWs) of varying frequencies and strengths are generated by such sources as the irradiations of high-voltage transmission lines, electrical appliances, microwave stations, and radio equipment
As mentioned previously, when protein molecules are exposed in an EMF or an electric fields (EFs), the dipole–dipole interaction between the neighboring amino acid residues in the protein molecules is changed into J ÑE .Ñp
We investigate the influences of EFs in EMFs on the energy transported by the soliton in protein molecules with single channels and three channels by using the numerical simulation method [107,108], respectively
Summary
Electromagnetic fields (EMFs) or waves (EMWs) of varying frequencies and strengths are generated by such sources as the irradiations of high-voltage transmission lines, electrical appliances, microwave stations, and radio equipment. Animals or humans are not measurably affected by EMFs unless they come in close contact with high-voltage transmission lines, research should focus more on the proliferation of microwaves and radio waves and their influences on health. The rapidly increasing usage of electrical appliances, microwave instruments, cell phones, and other electromagnetic devices has led to expansive distribution of EMFs in our environment In this case, it is necessary to study and release the biological effects of EMFs and their influences on the health of human beings and animals. It is necessary to study and release the biological effects of EMFs and their influences on the health of human beings and animals This need suggests that investigations should focus on the biological effects of EMFs—in particular, the mechanisms in depth through the latest ideas and methods in theoretical analyses and experimental measurements. We reveal the mechanism of influence of EMFs on energy transport in protein molecules and further study the properties of this mechanism
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