Abstract
The origin and potential role of chiral asymmetry remain one of the most exciting issues in biology. In this paper we review the chirality of biological macromolecules, starting at the level of single molecules and continuing to the level of supramolecular assemblies. We discuss the physical and chemical consequences of the presence of chirality and their role in the self-organization and formation of structural hierarchies in cells. Homochirality may serve as an essential factor that invokes mechanisms required to control the formation of discrete structural hierarchies in macromolecules and macromolecular assemblies. Symmetry is of fundamental importance not only for all molecular biology as a systemic factor of its organization but also for pharmacology, as well as a systemic factor of drug stereospecificity.
Highlights
Over the past decades and especially in recent years, with the advent of the latest physical and molecular biological research methods, as well as computer processing and analysis methods, many review papers concerning intra- and supramolecular protein structures have been published
It is known that the homochirality of the L-amino acids included in proteins ensures the stereospecificity of complementary interactions and minimizes the amount of information required for unambiguous coding of amino acid sequences by nucleic acids [39]
The chirality of monomers that make up the basis of informationally determined proteins and nucleic acids is usually perceived as an irrational episode in a reasonable evolutionary process, as a “payment” for the unique ability of carbon to form a huge number of inorganic and organic compounds that harmoniously bind the structures and functions of living systems
Summary
Over the past decades and especially in recent years, with the advent of the latest physical and molecular biological research methods, as well as computer processing and analysis methods, many review papers concerning intra- and supramolecular protein structures have been published. The chirality of monomers that make up the basis of informationally determined proteins and nucleic acids is usually perceived as an irrational episode in a reasonable evolutionary process, as a “payment” for the unique ability of carbon to form a huge number of inorganic and organic compounds that harmoniously bind the structures and functions of living systems. We propose to consider the structural details and hierarchies of protein structures based on a single physicochemical symmetry principle—their chirality. Such a description, based on the concept of a sequential change in the sign of chirality in differentscale protein structures, allows formalizing the “vertical” discreteness of protein structures as molecular machines by one order parameter. We consider the hierarchical structures of proteins as chiral details of their constructions
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