This theory of electromagnetic biomolecular interaction between biomolecules can integrate as another layer in a more extended electromagnetic information process (the mind!) in biosystems.
" It is evident that macromolecular interactions involve the transfer of energy. It has been proposed in the literature that the vibrational energy transfer is unlikely to occur 'because the typical time scale of vibrational relaxation (in order of few pica seconds) is much shorter than that of the resonant intermolecular vibrational energy transfer'. Here we present a concept, the so-called Resonant Recognition Model (RRM), which is based on a possibility of the resonant electromagnetic (EM) energy transfer between interacting molecules. The hypothesis of the possibility of EM energy transfer instead of the vibrational one can elucidate the nature of much faster molecular interactions (higher resonant frequencies)."
Firstly the authors point out that there are conformational changes in proteins that consists in formation of folds, twisting or compression of protein polypeptide chains, and because this displace electric charges of the surface, electromagnetic fields of particular frequencies can interact with these vibrations, this could happen with EMF in de range of the audio frequencies. In the range of RF EMF they could interact as "piezoelectric resonance" with defects and inhomogeneities of the substance.
They point out that each interaction between biomolecules involves energy transfer and that these interactions are highly selective, while with the existing model of key-and-lock it can be observed that the spatial complementarity is not selective enough. On the other hand light of specific frequencies induce or modulate biological processes and in some proteins is demonstrated that the frequency selectivity of this absorption is defined by the amino acid sequence.
So the authors propose that protein interaction is a resonant energy transfer between the interacting molecules with specific frequency for each interaction, they take in consideration that proteins have conduction or semi-conduction properties so a charge moving through the protein backbone (passing different energy stages caused by different amino acid side group) can produce conditions for electromagnetic generation or absorption. They estimate that the electromagnetic frequencies will be in infrared, visible and ultraviolet range of light.
To predict and interpret these frequencies they propose the Resonant Recognition Model where protein primary structure is represented as a numerical series by assigning to each amino acid a physical parameter value relevant to the proteins biological activity (the energy of the delocalised electrons of each amino acid). These data is later analysed by digital signal analysis methods, Fourier and Wavelet Transform (The n-th point in the spectral function corresponds to the frequency).
They also extract common spectral characteristics of sequences having the same or similar biological function (the peak frequencies), it must be exist only one peak in a group of protein sequences sharing the same biological function and no significant peak must exists for biologically unrelated protein sequences (peak frequencies are different for different biological functions).
There are experimental evidence that protein sequences with common biological function have common frequency components and also that the proteins and their target have the same characteristic frequency in common.
There are also experimental evidence of effects of applied light on biological systems (at very low intensities, this section of the web is dedicated to those studies).
The author continue speaking about "hot spots" (amino acids that are most affected by the change of amplitude of the characteristic peak frequency and that are found spatially clustered in the protein 3-D structure in and around the protein active site) and the prediction of protein active sites using the continuous wavelet transform. And they conclude with some experimental investigation of electromagnetic field interaction with proteins.
Last modified on 15-Mar-16