[Cotranslational, cosecretory protein folding and its renaturation from a denatured state].
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.
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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
D008051:Lipid Bilayers; D005914:Globins
Kotranslitsionnoe, kosekretornoe svorachivanie belka i ego renaturatsiiiz denaturirovannogo sostoianiia.