[Structure and organization of class I interferon molecules]. / Struktura i organizatsiia molekul interferonov I klassa.

The regular structure of class I interferon molecules was proposed using the new method of protein structure investigation--the comparative analysis of amino acids codon roots. It was found out that IFN-alpha and IFN-omega molecules are formed of 5 repeats. Each repeat can be divided into two parts or blocks with regular (alpha-spiral, block A) and irregular (parts of molecules between alpha-spirals, block B) structures. Localization of blocks A and B in IFN-alpha molecules has good correlation with the models of secondary structure organization of IFN-alpha. It is supposed that such a structure of IFN molecules is formed in the evolution process as a result of multiplication of IFN primary gene.

[Hidden symmetry of peptide and protein primary structures]. / Skrytaia simmetriia pervichnykh struktur peptidov i belkov.

The internal symmetry of peptide chains was considered. To identify symmetrically located equivalent amino acids, the signatures method and the code of amino acid codon roots were applied. There was revealed the hidden symmetry of amino acid sequences of peptides and proteins as well as of their active centres. Amino acids having common codon roots in primary (and supposedly in the spatial "biologically active") molecular structures, are located symmetrically. Definition of local symmetry of peptide chains was proposed to use as one of the elements of complex analysis to determine location of molecular active centres.

[The structural organization of interferon molecules as precursors of immuno- and neuroactive oligopeptides]. / Strukturnaia organizatsiia molekul interferonov kak predshestvennikov immuno- i neiroaktivnykh oligopeptidov.

The oligopeptides effecting signalling functions are postulated to emerge from protein precursors by limited proteolytic cleavage in close vicinity to appropriate cell receptors. A variety of immunological activities of interferons are probably mediated by this mechanism. The C-terminal tripeptides liberated from IFN-alpha in limited proteolysis reactions may result in a variety of polarins eliciting a wide spectrum of immunoregulatory effects, which in combination with the antiviral activity of IFN are responsible for effective defense mechanisms in the organism.