Environmental Light and Its Relationship with Electromagnetic Resonances of Biomolecular Interactions, as Predicted by the Resonant Recognition Model
Abstract
:1. Introduction
- 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
- 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.
3. Results
4. Discussion
4.1. Functional Super Families
4.2. Water Absorption
4.3. Artificial Light
5. Conclusions
Acknowledgments
Author Contributions
Conflicts of Interest
References
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RRM Frequency | Nano Meters | Functional Group | Super Family |
---|---|---|---|
0.002 | 100 K | Circumsporosoite, PfEMP1, EBA, ICHIT (malaria) | |
0.0234 | 20 K | Hemoglobin | |
0.027 | 7444 | Protein A-VHIII | Tumor regulation |
0.031 | 6484 | Antitumor agents (TNF + IL-2 + IFN-beta + human M-CSF) | |
0.0313 | 6422 | Oncogenes | |
0.039 | 5154 | IL-1 | |
0.0430 | 4674 | Phospholipases | |
0.0439 | 4579 | Insulin multimer | |
0.0446 | 4508 | Glucocorticoide receptors | |
0.0459 | 4379 | Homeo box proteins | |
0.0488 | 4119 | Enhancers | |
0.049 | 4102 | TNF receptors | |
0.051 | 3941 | TNFs | |
0.054 | 3722 | Proto-oncogenes | |
0.0590 | 3407 | Cytochrome B | |
0.062 | 3242 | EGF–EGF receptor | |
0.0703 | 2859 | Neurotoxins | |
0.0781 | 2574 | Operators | |
0.0820 | 2451 | Interferons | |
0.0820 | 2451 | Myoglobins | |
0.0839 | 2396 | Bacterial repressors | Viral–bacterial infection |
0.0947 | 2122 | Heat shock proteins | |
0.096 | 2094 | Tubulins A + B | |
0.0990 | 2030 | Repressors | |
0.1054 | 1907 | Phage repressors | |
0.110 | 1827 | EBA-RBC (malaria interaction with red blood cells) | |
0.115 | 1748 | Myxoma virus | |
0.162 | 1241 | IGFBP | |
0.173 | 1162 | Telomere binding | |
0.186 | 1081 | HIV envelope | |
0.188 | 1069 | Telomere | |
0.2363 | 851 | Chymotrypsins | |
0.281 | 715 | Purple (bacteria) | |
0.285 | 705 | TERT + telomerase RNA + progerin | Growth |
0.288 | 698 | EGFs | |
0.289 | 695 | Growth hormons + NGF + proliferins | |
0.2929 | 686 | Growth factors (CSF + EGF + IL-2) | |
0.297 | 678 | CSF, Ubiquitins, EPA | |
0.300 | 670 | IL-2, IL-4, IL-6 | |
0.308 | 653 | IL-2—IL2 receptor | |
0.3203 | 628 | Glucagons | |
0.3281 | 613 | Lysozymes | Enzymes |
0.3400 | 591 | Myosins | |
0.3437 | 585 | Promoters | |
0.3447 | 583 | Trypsins | |
0.346 | 581 | Red (rhodopsin) | |
0.35 | 574 | RNA polymerase | |
0.355 | 566 | Green (rhodopsin and chlorophylls) | |
0.3555 | 565 | Protease inhibitors | |
0.3770 | 533 | Proteases | |
0.379 | 530 | Flavodoxins | |
0.3828 | 525 | Insulin receptors | |
0.383 | 525 | Insulins | |
0.4040 | 498 | NGFs | |
0.4121 | 488 | Amylases | |
0.4297 | 468 | Kinases | |
0.434 | 463 | Tubulins beta | Structural proteins |
0.4423 | 454 | Fibrinogens | |
0.449 | 448 | Tubulins alpha | |
0.4512 | 445 | FGFs, FGF receptors | |
0.453 | 444 | IL-12 | |
0.4609 | 436 | Serine proteases | |
0.4687 | 429 | SOS operators | |
0.475 | 423 | Blue (rhodopsin and bioluminescent proteins) | Blue |
0.4765 | 422 | Cytochrome C | |
0.4800 | 419 | Actins | |
0.4922 | 408 | ACH receptors | |
0.4922 | 408 | IGFs |
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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
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 StyleCosic, 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 StyleCosic, 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