The resonant recognition model (RRM) is a model of protein-protein and protein-DNA interaction based on a significant correlation between spectra of numerical presentation of the amino acid or nucleotide sequences and their biological activity. Having compared absorption characteristics of photosensitive proteins with their RRM spectral characteristics we obtained a linear correlation between the RRM frequency space and real frequency space, which determines a scaling factor between these two frequency spaces. On applying the RRM model to several groups of peptide growth factors, characteristic RRM frequencies were revealed and the corresponding real characteristic frequencies for these groups of growth factors were calculated using the scaling factor previously obtained. The real frequency characteristics of growth factors obtained in this way correspond with maxima in the action spectra of low-intensity light irradiation effects on cell proliferation.
This study is focused on experimental validation of our hypothesis proposed within the Resonant Recognition Model (RRM) [7], [8] that protein function can be modified by an applied electromagnetic radiation of defined frequency in a range of infra red (IR), visible and ultra violet (UV) light. This postulate is investigated here by applying the electromagnetic radiation (1140-1200 nm) to example of L-Lactate Dehydrogenase (LDH) protein and its biological activity is measured before and after the exposures. The presented methodology provides a possibility of enhancing the pharmaceutical and agricultural industries by amplifying drug potency via electromagnetic radiation.
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