Reveiw study: influence of electromagnetic radiation on enzyme activity and effects of synthetic peptides on cell transformation

With a large number of DNA and protein sequences already known, the crucial question is to find out how the biological function of these bio-molecules is "written" in the sequence of nucleotides or amino acids. Biological processes in any living organism are based on selective interactions between particular bio-molecules, mostly proteins. However, the rules governing the coding of the protein's biological function, i.e. its ability to selectively interact with other molecules, are still not elucidated. With the rapid accumulation of databases for protein primary structures, there is an urgent need for theoretical approaches that are capable of analysing protein structure-function relationships. The Resonant Recognition Model (RRM) (1) is one attempt to identify the selectivity of protein interactions within an amino acid sequence. The RRM approach (2,3) proposes that protein interactions are electromagnetic in nature and their selectivity is based on resonant energy transfer between the interacting molecules that occurs at the same frequency. Once this frequency is identified, it is possible to predict the functionally important "key" amino acids in the protein sequence as well as to design de novo proteins/peptides with desired biological functions. In this paper we present the RRM basic concepts and discuss its biological applications both theoretically and experimentally. A number of test examples are presented: protein (enzyme) activation using external electromagnetic radiation (EMR) of computationally defined wavelengths, and experimental evaluation of biological activity of de novo peptides designed using the RRM approach.