Quantum Foundations of Resonant Recognition Model

Abstract

Biomolecular recognition is open scientific problem, which has been investigated in many theoretical and experimental aspects. In that sense, there are encouraging results within Resonant Recognition Model (RRM), which is based on theory of information spectrum of macromolecules. The RRM concept is based on the finding that there is a significant correlation between spectra of the numerical presentation of amino acids in the primary structure of proteins and their biological activity. It has been found through an extensive research that proteins with the same biological function have a common RRM peak (wavenumber) in their numerical spectra, correlated to EM peak (frequency) by semi-empirical dispersion relation. This peak was found then to be a characteristic feature for protein biological function or interaction. The RRM model proposes that the selectivity of protein-target interactions is based on resonant energy transfer between interacting biomolecules and that this energy, EM in its nature, is in the frequency range of 10 13 to 10 15 Hz, which incorporates infra-red (IR), visible and a small portion of the ultra-violet (UV) radiation. In this paper, the quantum mechanical basis of the RRM model will be investigated using the solution in the simplified framework of Huckel-like theory of molecular orbits. Biological processes in living organisms are based on selective interactions between bio- molecules. These interactions are very specific and selective. This specificity is driven by the proteins, but it is still a puzzle where and how this specificity is written in the protein structure. Currently accepted explanation is that the specificity of protein interactions is written in the protein 3-D structure and it is based on key-and-lock fit between 3-D structure of the protein active side and interactive target. However, this fit in most cases is very loose, and it is difficult to believe that this is the solely important parameter for the extremely selective and specific recognitions/interactions between biomolecules. The RRM model is based on representation of the protein primary structure as a discrete signals by assigning to each amino acid, the electron excitation energy Em (1-4), which is calculated as a electron-ion interaction pseudopotential (EIIP values). Consequently, these numerical series are converted into Fourier spectrum by using Discrete Fourier transform (DFT). The coefficients in the discrete Fourier transform are defined as: N mk i N