title: [Interconnection between architecture of protein globule and disposition of conformational conservative oligopeptides in proteins from one protein family].
abstract: It was shown that selective interactions between helical segments of macromolecules can realize in globular proteins in the segments characterized by the same periodicities of charge distribution i.e. between conformationally conservative oligopeptides. It was found that in the macromolecules of alpha-helical proteins conformationally conservative oligopeptides are disposed at a distance being characteristic of direct interactions. For representatives of many structural families of alpha-type proteins specific disposition of conformationally conservative segments is observed. This disposition is inherent to a particular structural family. Disposition of conformationally conservative segments is not related to homology of the amino acid sequence but reflects peculiarities of native 3D-architectures of protein globules.
authors.forename: A V
authors.initials: AV
authors.lastname: Batianovskiĭ
authors.forename: I V
authors.initials: IV
authors.lastname: Filatov
authors.forename: V A
authors.initials: VA
authors.lastname: Namiot
authors.forename: N G
authors.initials: NG
authors.lastname: Esipova
authors.forename: I D
authors.initials: ID
authors.lastname: Volotovskiĭ
mesh_terms: D004798:Enzymes / Q000737:chemistry*; D008962:Models, Theoretical; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D004798:Enzymes; D009842:Oligopeptides