title: [Cotranslational, cosecretory protein folding and its renaturation from a denatured state].
abstract: On the basis of the available experimental data on structure, biosynthesis and secretion of globular proteins it is concluded that an alpha-helix is a starting conformation at formation of the native structure of any globular protein (alpha-helical model for initiation of protein folding). The structural invariant (clusterization of hydrophobic side chains on the alpha-helix surface) in the amino acid sequences of globular proteins is found which is predicted by alpha-helical model for the initiation of protein folding. The model predicts the pyramidization of the atoms C and N of peptide groups during the formation of spatial structure of proteins and a number of other effects that can be put to the experimental test. In the work the mechanism for protein translocation across membrane lipid bilayer is also suggested.
authors.forename: V I
authors.initials: VI
authors.lastname: Lim
mesh_terms: D000595:Amino Acid Sequence; D001692:Biological Transport; D005914:Globins / Q000737:chemistry; D008051:Lipid Bilayers; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D008051:Lipid Bilayers; D005914:Globins
vernacular_title: Kotranslitsionnoe, kosekretornoe svorachivanie belka i ego renaturatsiiiz denaturirovannogo sostoianiia.