[Structure of ribosomal proteins. Prediction of the tertiary structure of proteins from small 30S Escherichia coli ribosomal subparticles].
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Biomedical subjects
Publications and source records attributed to V I Lim.
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It is shown within the framework of stereochemical modeling that disruption of water shells of proteins and nucleic acids is confronted by significant kinetic barriers caused by the breaking of hydrogen bonds. The structure of the water shells is dictated by the surface of proteins and nucleic acids, therefore the kinetic barriers due to disruption of the water shell are strongly distinct from each other on different parts of the shell. This, in turn, means that the probability of participation of different parts of the protein and nucleic acid surfaces in intermolecular interactions should be varied through a wide range, i.e. the water shell should strengthen selectivity of molecular recognition.
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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