title: [Geometric complementarity of the primary structures of histone molecules H2A, H2B, H3, H4 and several possible consequences of this phenomenon].
abstract: The paper treats of the correlations between the position geometry of the extended successions of the residue of basic amino acids and those nonbearing any positive charge along the polypeptide chains of the histone H2A, H2B, H3, H4 molecules forming nucleosomes protein frame. The number of histone packing variants in the tetramere conforming to the conditions of the revealed complementarity reached the value of 10(4), and in respect to histone octamere--10(8). A hypothesis was put forward on structural heterogeneity of nucleosomes (of functional significance) the choice of whose protein frame packing variant could be realized by the mechanisms of allosteric regulation of the primary structure of DNA molecule section serving as the nucleosome element.
mesh_terms: D002875:Chromosomes / Q000648:ultrastructure; D006657:Histones; D011487:Protein Conformation
chemical_list: D006657:Histones
vernacular_title: O geometricheskoĭ komplementarnosti pervichnykh struktur molekul gistonov H2A, H2B, H3, H4 i nekotorykh vozmozhnykh sledstviiakh étogo fenomena.