One of the basic physical concepts of molecular biophysics "protein-machine" is based on the ideas of a hierarchical arrangement of protein macromolecules and the presence of "selected mechanical degrees of freedom" in them structurally associated with the formation of secondary and tertiary structures in folding processes. We develop a concept according to which the structural hierarchy and the selected mechanical degrees of freedom are formed by intramolecular and intermolecular alternating chiral structures, helices and supercoils. Regular alternation of the chirality sence is revealed in transitions from the lowest to higher level of structural and functional organization in protein macromolecules where it is L-D- L-D. A periodic table of supercoiled structures in proteins is made and a thermodynamic folding model that takes into account alternating chiral structuring is proposed. The possibility of representing a system of biological macromolecules as a periodic system is discussed according to chiral antiphase of structural levels in proteins and DNA macromolecules.
chirality, nucleic acids, proteins, structural hierarchies, folding, periodic system of biomacromolecules
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