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Article

Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model

1
College of Science, Engineering and Health, RMIT University, La Trobe Street, Melbourne, Victoria 3000, Australia
2
AMALNA Consulting, 46 Second St., Black Rock, Victoria 3193, Australia
*
Author to whom correspondence should be addressed.
Int. J. Environ. Res. Public Health 2016, 13(7), 647; https://doi.org/10.3390/ijerph13070647
Submission received: 23 May 2016 / Revised: 25 June 2016 / Accepted: 27 June 2016 / Published: 29 June 2016

Abstract

:
The meaning and influence of light to biomolecular interactions, and consequently to health, has been analyzed using the Resonant Recognition Model (RRM). The RRM proposes that biological processes/interactions are based on electromagnetic resonances between interacting biomolecules at specific electromagnetic frequencies within the infra-red, visible and ultra-violet frequency ranges, where each interaction can be identified by the certain frequency critical for resonant activation of specific biological activities of proteins and DNA. We found that: (1) the various biological interactions could be grouped according to their resonant frequency into super families of these functions, enabling simpler analyses of these interactions and consequently analyses of influence of electromagnetic frequencies to health; (2) the RRM spectrum of all analyzed biological functions/interactions is the same as the spectrum of the sun light on the Earth, which is in accordance with fact that life is sustained by the sun light; (3) the water is transparent to RRM frequencies, enabling proteins and DNA to interact without loss of energy; (4) the spectrum of some artificial sources of light, as opposed to the sun light, do not cover the whole RRM spectrum, causing concerns for disturbance to some biological functions and consequently we speculate that it can influence health.

1. Introduction

It is well known that the life on Earth has been sustained by the electromagnetic energy from sunlight. In primitive organisms and plants the sunlight directly influences biological processes, while, in more complex organisms, it has a more indirect role. In these organisms, due to their more complex structures, sunlight cannot penetrate into each cell, therefore, they have to create their own “internal sun” energy to drive the selectivity of biological processes in their cells, in the same manner as they were initially sustained by the sun [1,2].
The selectivity (specificity) of biological processes is driven by the information contained within linear macromolecules: DNA and proteins. While information in DNA is written within the long sequences using different combinations of four different nucleotides, information in proteins is also written within long sequences, but using different combinations of 20 amino acids. While DNA carries the complete backup information of any organism, proteins are macromolecules that read the necessary parts of DNA information to actually perform all selective biological activity through a number of very specific interactions. The Resonant Recognition Model (RRM) model proposes that macromolecular selective interactions are based on electromagnetic resonant energy transfer between macromolecules in the range of infra-red, visible and ultra-violet light, and, thus, could mimic the specificity enabled by different frequencies (wavelengths) of sunlight [3,4]. By applying RRM, it is possible to identify and calculate relevant frequencies, critical for resonant activation of specific biological activities of proteins and DNA [5,6,7,8,9,10,11].
Here, we discuss:
  • whole RRM spectrum for different biological functions of proteins and DNA;
  • grouping of different biological functions into super families;
  • comparison of RRM spectrum with the water absorption spectrum, spectrum of sunlight and spectrum of some artificial sources of light.

2. Materials and Methods

Resonant Recognition Model

RRM is based on the findings that certain periodicities within the distribution of energy of delocalized electrons along a protein (DNA/RNA) molecule are critical for protein (DNA/RNA) biological function and/or interaction with their targets [3,4,12]. If charge transfer through these macromolecules is introduced, then the charge moving through the macromolecular backbone can produce electromagnetic radiation, absorption and resonance with spectral characteristics corresponding to the energy distribution [3,4,5,6,7,8].
RRM enables the calculation of these spectral characteristics, by assigning each amino acid a physical parameter representing the energy of delocalized electrons of each amino acid. Comparing Fourier spectra for these energy distributions, using cross-spectral function, it has been found that proteins sharing the same biological function/interaction share the same periodicity (frequency) within the energy distribution along the macromolecule [3,4]. Furthermore, it has been shown that interacting proteins and their targets share the same characteristic frequency, but have an opposite phase at a characteristic frequency [3,4,12]. Thus, it has been proposed that the RRM frequencies characterize, not only a general function, but also recognition and interaction between the particular macromolecule and its target, which can then be considered to be resonant recognition. This could be achieved with resonant energy transfer between the interacting macromolecules through oscillations of a physical field, which is electromagnetic in nature. Since there is evidence that proteins and DNA have certain conducting or semi-conducting properties, a charge moving through the macromolecular backbone and passing different energy stages, caused by different amino acid or nucleotide side groups, can produce sufficient conditions for a specific electromagnetic radiation or absorption. The frequency ranges of this field depend on the charge velocity. RRM proposes that the charge is travelling through the macromolecular backbone at an estimated velocity of 7.87 × 105 m/s [3,4]. For this velocity, and with the distance between amino acids in a protein molecule of 3.8 Å, the frequency of protein interactions was estimated to be in the range of 1013 Hz and 1015 Hz. Therefore, the estimated frequency range for both amino acid and nucleotide macromolecules includes infra-red, visible and ultra-violet light. To support this idea, we compared our computational predictions with a number of published experimental results [3,4,8]:
  • Laser light growth promotion of cells, by using the particular frequencies of light to produce the similar effect to that of growth factor proteins;
  • chymotrypsin activation (increase of enzyme activity) achieved by laser light radiation in a range of 850–860 nm;
  • activation of highly homologous plant photoreceptors which, although being very homologous, absorb different wavelengths of light;
  • photo activated proteins, e.g., rhodopsin, flavodoxin, etc.
These comparisons have shown a strong linear correlation between frequencies, as calculated using the RRM method and experimentally measured characteristic frequencies, with a slope factor of K = 201 [3,4,8]. This finding is in parallel with the frequency range previously associated with the RRM numerical frequency spectrum, which has been calculated from the charge velocities through the protein backbone. This correlation can be represented as following:
λ = K/frrm
where λ is the wavelength of light irradiation in nm, which can influence a particular biological process, frrm is a RRM numerical frequency, and K is coefficient of this linear correlation.
We applied this concept to a number of proteins and DNA examples [3,4,5,6,7,8]. The concept has been also experimentally tested by predicting the electromagnetic frequencies for l-Lactate Dehydrogenase [8], whereby radiating l-Lactate Dehydrogenase with predicted calculated electromagnetic frequencies achieved a significant change in enzyme activity. The concept has also been tested independently on experimental measurements of photon emission from dying melanoma cells [9], on photon emission from lethal and non-lethal Ebola strains [10], as well as on the classic signaling pathway, JAK-STAT, traditionally composed of nine sequential protein interactions [11].
Keeping all this in mind, we propose that the RRM concept is an excellent predictor for the selective interactions, biological processes and pathways of proteins and DNA in living cells. In our previous work, we have calculated a large number of specific frequencies for different protein and DNA biological functions and interactions. These frequencies, and related functions, are presented in Table 1.

3. Results

We applied the RRM model to a large number of protein and DNA functional groups, and the identified characteristic RRM frequencies are presented in Table 1. The chosen protein and DNA sequences have been predominantly selected based on the availability of sequences, proven biological functions and existing experimental results. Therefore, there is a possibility that new functional groups and related RRM frequencies will appear in future research.
It can be observed from the calculated RRM frequencies, that there are interesting groupings of biological functions into functional super families. For example, it can be observed that protein and DNA functions that are related to the uncontrolled cell growth super family (like oncogenes, antitumor agents, TNFs, etc.), are all within the frequency range between 0.031 and 0.054, as highlighted in red, in Table 1. Similarly, the super family of viral and bacterial infections are grouped together and highlighted in orange, the super family related to controlled growth is highlighted in yellow, while the super family related to enzyme activity is highlighted in green, as presented in Table 1. It appears that there are two smaller super families: Structural proteins, highlighted in blue, and proteins related to blue light absorption/emission, highlighted in violet. In addition, there are other functional groups that cannot be grouped into the super families at this point in time, but, with more knowledge on protein and DNA sequences and their functions, there are possibilities for more super families to be identified.
The results presented in Table 1 have been also presented graphically in Figure 1, where each RRM frequency range of 0.01 is presented with number of functions within that range. This graphical presentation enables a better visualization of functional groupings of protein and DNA macromolecules, based on RRM frequencies. All identified super families have been colored in accordance to the colors used in Table 1.
Based on the RRM principle, as described in Materials and Methods section, the numerical RRM frequencies represent oscillations of electromagnetic fields, which are relevant for specific biological functions/interactions. The frequencies of these electromagnetic oscillations are calculated in nm for each biological function, and are presented in Table 1, column 2. For each 0.1 of the RRM frequency range, as presented in Figure 1, the corresponding frequencies of electromagnetic oscillations have been calculated in nm and presented along the X axis in Figure 1.

4. Discussion

4.1. Functional Super Families

As presented above, the protein and DNA sequences can be grouped into functional super families, based on the calculated RRM frequencies. The most interesting result is that there are distinct RRM characteristics for uncontrolled and controlled cell growth, which presents an enormous opportunity for understanding cell transformation and cell growth control. Having such characteristics at the molecular level provides a new aspect to influence uncontrolled cell growth and consequently combat cancer formation and growth. Some preliminary results have experimentally shown that it is possible to use the RRM to design peptides that can interfere with oncogenic transformation [13,14]. RRM proposes that the characteristic of uncontrolled cell growth is in a specific range of electromagnetic radiation, which has been proved by experimental measurements with cancer tissue [9,15]. In addition, the design of bioactive peptides, using the RRM, have been experimentally tested on examples of cell growth control [16] and vaccine development [17], as well as electromagnetic radiation, as predicted by RRM, can interfere with infections such as malaria [18] and Ebola [10].

4.2. Water Absorption

It can be observed that the whole spectrum of frequencies, as predicted by RRM to be relevant for the biological activity of proteins and DNA, also covering the same spectrum as the spectrum of sunlight on the Earth’s surface, as represented by the yellow line in Figure 2 [19]. This finding was as expected, since sunlight sustains all life processes on Earth. This implies that protein and DNA activity is mimicking the role of the sun within the biological functions of the cells.
It is also important to note that all biological processes in living cells occur in a water medium, which is only transparent for electromagnetic frequencies in the spectrum encompassing mostly visible light, just as predicted by RRM. This means the water medium enables electromagnetic radiation of these frequencies to be transferred between macromolecules without any loss of energy and, therefore, maximizing the efficiency of these interactions.

4.3. Artificial Light

The frequency range for biological functions has been found to be the same as the frequency range of sunlight on Earth, as described above. This reinforces the fact that life is sustained by the energy from sunlight. This also means that environmental sunlight is natural source of life on Earth. Humans, however, are spending more and more time under artificial lights, which may not have the same spectral characteristics as sunlight and, therefore, may induce a debalance in some biological functions. The spectrums of some artificial light sources have been presented in Figure 2 [19]. It is interesting to note that incandescent light, as represented by the purple line, has a similar spectrum shape as sunlight. In contrast, LED (light-emitting diode) light, as represented with the blue line, and CFL (compact fluorescent light) light, as represented by the green line, have distinct peaks at certain frequencies within the spectrum, while they are missing many of the other frequencies from the sunlight spectrum.
We have compared the spectrums of LED and CFL artificial lights with the frequencies of particular biological functions, as calculated by the RRM model. It can be observed that the artificial lights have strong radiation relevant to enzymes and that control growth activity, while they are missing frequencies related to tumor regulation and viral-bacterial infections. We speculate that these findings could suggest the possibility that, under such artificial lights, tumor regulation could be affected. In addition, we speculate that lack of light frequencies in the range of bacterial and viral infection control could lead to a higher susceptibility to these infections. Although, the majority of biological functions within the human organism are protected from electromagnetic radiation within the observed spectrum by skin and clothes, these artificial lights might still cause some distortions to biological functions in humans due to the lack of a full spectrum of sunlight. For example, there is experimental evidence that the specific photon energies of the weak magnetic field of the LED wavelength pulses are stored in malignant cells [20].

5. Conclusions

Here, for the first time, environmental light electromagnetic radiation was investigated as a source and influence on biomolecular interactions, related biological functions and consequent health effects. The relationship between our theoretical model, RRM, and sunlight’s ability to sustain of life, gives a possible explanation of how life processes may have evolved and are controlled in more complex organisms, where the sunlight cannot penetrate all cells and cellular processes. In addition, although biological processes are currently regarded as a large number of different events, we have shown that they are grouped in a relatively small number of general functions, enabling a simpler approach in understanding macromolecular interactions, biological functions and related health effects. In that light, the role of water and the possible influence of artificial light on biological processes have been shown. Keeping all this in mind, we can conclude that the Resonant Recognition Model (RRM) is a powerful tool in the analysis of protein and DNA functions/interactions, which are proposed to be based on resonant electromagnetic energy transfer.

Acknowledgments

This work was supported by AMALNA Consulting.

Author Contributions

Irena Cosic conceived and conceptualized this research, Drasko Cosic performed all calculations, Drasko Cosic and Katarina Lazar analyzed all results, all authors have been equally involved in writing the paper.

Conflicts of Interest

The authors declare no conflict of interest.

References

  1. Cifra, M.; Brouder, C.; Nerudova, M.; Kucera, O. Biophotons, coherence and photocount statistics: A critical review. J. Lumin. 2015. [Google Scholar] [CrossRef]
  2. Cifra, M.; Pospisil, P. Ultra-weak photon emission from biological samples: Definition, mechanisms, properties, detection and applications. J. Photochem. Photobiol. B Biol. 2014, 139, 2–10. [Google Scholar] [CrossRef] [PubMed]
  3. Cosic, I. Macromolecular bioactivity: Is it resonant interaction between macromolecules? IEEE Trans. Biomed. Eng. Theory Appl. 1994, 41, 1101–1114. [Google Scholar] [CrossRef] [PubMed]
  4. Cosic, I. The Resonant Recognition Model of Macromolecular Bioactivity: Theory and Applications; Birkhauser Verlag: Basel, Switzerland, 1997. [Google Scholar]
  5. Cosic, I.; Lazar, K.; Cosic, D. Prediction of Tubulin resonant frequencies using the Resonant Recognition Model (RRM). IEEE Trans. NanoBiosci. 2015, 12, 491–496. [Google Scholar] [CrossRef] [PubMed]
  6. Cosic, I.; Cosic, D.; Lazar, K. Is it possible to predict electromagnetic resonances in proteins, DNA and RNA? Nonlinear Biomed. Phys. 2015. [Google Scholar] [CrossRef]
  7. Cosic, I. Resonant Recognition Model of Protein-Protein and Protein-DNA Recognition, in Bioinstrumentation and Biosensors; Marcel Dekker Inc.: New York, NY, USA, 1990; pp. 475–510. [Google Scholar]
  8. Vojisavljevic, V.; Pirogova, E.; Cosic, I. The effect of electromagnetic radiation (550 nm–850 nm) on i-Lactate Dehydrogenase Kinetics. Int. J. Radiat. Biol. 2007, 83, 221–230. [Google Scholar] [CrossRef] [PubMed]
  9. Dotta, B.T.; Murugan, N.J.; Karbowski, L.M.; Lafrenie, R.M.; Persinger, M.A. Shifting wavelength of ultraweak photon emissions from dying melanoma cells: Their chemical enhancement and blocking are predicted by Cosic’s theory of resonant recognition model for macromolecules. Naturwissenschaften 2014, 101. [Google Scholar] [CrossRef] [PubMed]
  10. Murugan, N.J.; Karbowski, L.M.; Persinger, M.A. Cosic’s Resonance recognition model for protein sequences and photon emission differentiates lethal and non-lethal ebola strains: Implications for treatment. Open J. Biophys. 2014, 5, 35–43. [Google Scholar] [CrossRef]
  11. Karbowski, L.M.; Murugan, N.J.; Persinger, M.A. Novel Cosic resonance (standing wave) solutions for components of the JAK-STAT cellular signalling pathway: A convergence of spectral density profiles. FEBS Open Biol. 2015, 5, 245–250. [Google Scholar] [CrossRef] [PubMed]
  12. Cosic, I.; Cosic, D.; Lazar, K. Analysis of tumor necrosis factor function using the resonant recognition model. Cell Biochem. Biophys. 2016, 74, 175–180. [Google Scholar] [CrossRef] [PubMed]
  13. Istivan, T.; Pirogova, E.; Gan, E.; Almansour, N.; Coloe, P.; Cosic, I. Biological effects of a De Novo designed myxoma virus peptide analogue: Evaluation of cytotoxicity on tumor cells. PLoS ONE 2011, 6, e24809. [Google Scholar] [CrossRef] [PubMed]
  14. Almansour, N.; Pirogova, E.; Coloe, P.; Cosic, I.; Istivan, T. Investigation of cytotoxicity of negative control peptides vs. bioactive peptides on skin cancer and normal cells: A comparative study. Future Med. Chem. 2012, 4, 1553–1565. [Google Scholar] [CrossRef] [PubMed]
  15. Peidaee, P.; Almansour, N.M.; Pirogova, E. In vitro evaluation of low-intensity light radiation on murine melanoma (B16F10) cells. Med. Biol. Eng. Comput. 2016, 54, 325–332. [Google Scholar] [CrossRef] [PubMed]
  16. Cosic, I.; Drummond, A.E.; Underwood, J.R.; Hearn, M.T.W. In vitro inhibition of the actions of basic FGF by a novel 16 amino acid peptides. Mol. Cell. Biochem. 1994, 130, 1–9. [Google Scholar] [CrossRef] [PubMed]
  17. Krsmanovic, V.; Biquard, J.M.; Sikorska-Walker, M.; Cosic, I.; Desgranges, C.; Trabaud, M.A.; Whitfield, J.F.; Durkin, J.P.; Achour, A.; Hearn, M.T.W.; et al. Investigation into the Cross-reactivity of Rabbit Antibodies Raised against nonhomologous Pairs of Synthetic Peptides Derived from HIV-1 gp120 proteins. J. Peptide Res. 1998, 52, 410–412. [Google Scholar] [CrossRef]
  18. Cosic, I.; Caceres, J.L.H.; Cosic, D. Possibility to interfere with malaria parasite activity using specific electromagnetic frequencies. EPJ Nonlinear Biomed. Phys. 2015. [Google Scholar] [CrossRef]
  19. Katz, B. How to Light Art Glass—Lighting Art Guide. 2015. Available online: https://bernardkatz.com (accessed on 28 June 2016).
  20. Karbowski, L.M.; Murugan, N.J.; Persinger, M.A. Experimental evidence that specific photon energies are “Stored” in malignant cells for an hour: The synergism of weak magnetic Field-LED wavelength pulses. Biol. Med. 2016, 8, 1–8. [Google Scholar]
Figure 1. Number of functional groups within each Resonant Recognition Model (RRM) frequency range of 0.01. X axis represent RRM frequency in steps of 0.01, as well as corresponding electromagnetic frequency in nm. Y axis represent number of functional groups. Names of functional groups are noted above each bar. Super families are colored as in Table 1.
Figure 1. Number of functional groups within each Resonant Recognition Model (RRM) frequency range of 0.01. X axis represent RRM frequency in steps of 0.01, as well as corresponding electromagnetic frequency in nm. Y axis represent number of functional groups. Names of functional groups are noted above each bar. Super families are colored as in Table 1.
Ijerph 13 00647 g001
Figure 2. Diagram of the spectrum a LED lamp (blue), a CFL (green) and an incandescent (purple) superimposed the solar spectrum (yellow).
Figure 2. Diagram of the spectrum a LED lamp (blue), a CFL (green) and an incandescent (purple) superimposed the solar spectrum (yellow).
Ijerph 13 00647 g002
Table 1. Characteristic Resonant Recognition Model (RRM) frequencies for different biological functions of protein and DNA macromolecules. Column 1 represents the numerical RRM frequency. Column 2 represents the corresponding electromagnetic radiation in nm. Column 3 represents name of functional group of proteins and DNA. Column 4 represents super family of number of functional groups, which are also highlighted in different colors.
Table 1. Characteristic Resonant Recognition Model (RRM) frequencies for different biological functions of protein and DNA macromolecules. Column 1 represents the numerical RRM frequency. Column 2 represents the corresponding electromagnetic radiation in nm. Column 3 represents name of functional group of proteins and DNA. Column 4 represents super family of number of functional groups, which are also highlighted in different colors.
RRM FrequencyNano MetersFunctional GroupSuper Family
0.002100 KCircumsporosoite, PfEMP1, EBA, ICHIT (malaria)
0.023420 KHemoglobin
0.0277444Protein A-VHIIITumor regulation
0.0316484Antitumor agents (TNF + IL-2 + IFN-beta + human M-CSF)
0.03136422Oncogenes
0.0395154IL-1
0.04304674Phospholipases
0.04394579Insulin multimer
0.04464508Glucocorticoide receptors
0.04594379Homeo box proteins
0.04884119Enhancers
0.0494102TNF receptors
0.0513941TNFs
0.0543722Proto-oncogenes
0.05903407Cytochrome B
0.0623242EGF–EGF receptor
0.07032859Neurotoxins
0.07812574Operators
0.08202451Interferons
0.08202451Myoglobins
0.08392396Bacterial repressorsViral–bacterial infection
0.09472122Heat shock proteins
0.0962094Tubulins A + B
0.09902030Repressors
0.10541907Phage repressors
0.1101827EBA-RBC (malaria interaction with red blood cells)
0.1151748Myxoma virus
0.1621241IGFBP
0.1731162Telomere binding
0.1861081HIV envelope
0.1881069Telomere
0.2363851Chymotrypsins
0.281715Purple (bacteria)
0.285705TERT + telomerase RNA + progerinGrowth
0.288698EGFs
0.289695Growth hormons + NGF + proliferins
0.2929686Growth factors (CSF + EGF + IL-2)
0.297678CSF, Ubiquitins, EPA
0.300670IL-2, IL-4, IL-6
0.308653IL-2—IL2 receptor
0.3203628Glucagons
0.3281613LysozymesEnzymes
0.3400591Myosins
0.3437585Promoters
0.3447583Trypsins
0.346581Red (rhodopsin)
0.35574RNA polymerase
0.355566Green (rhodopsin and chlorophylls)
0.3555565Protease inhibitors
0.3770533Proteases
0.379530Flavodoxins
0.3828525Insulin receptors
0.383525Insulins
0.4040498NGFs
0.4121488Amylases
0.4297468Kinases
0.434463Tubulins betaStructural proteins
0.4423454Fibrinogens
0.449448Tubulins alpha
0.4512445FGFs, FGF receptors
0.453444IL-12
0.4609436Serine proteases
0.4687429SOS operators
0.475423Blue (rhodopsin and bioluminescent proteins)Blue
0.4765422Cytochrome C
0.4800419Actins
0.4922408ACH receptors
0.4922408IGFs

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MDPI and ACS Style

Cosic, I.; Cosic, D.; Lazar, K. Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model. Int. J. Environ. Res. Public Health 2016, 13, 647. https://doi.org/10.3390/ijerph13070647

AMA Style

Cosic I, Cosic D, Lazar K. Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model. International Journal of Environmental Research and Public Health. 2016; 13(7):647. https://doi.org/10.3390/ijerph13070647

Chicago/Turabian Style

Cosic, Irena, Drasko Cosic, and Katarina Lazar. 2016. "Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model" International Journal of Environmental Research and Public Health 13, no. 7: 647. https://doi.org/10.3390/ijerph13070647

APA Style

Cosic, I., Cosic, D., & Lazar, K. (2016). Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model. International Journal of Environmental Research and Public Health, 13(7), 647. https://doi.org/10.3390/ijerph13070647

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