Biopolym. Cell. 1988; 4(2):79-85.
Structure and Function of Biopolymers
Effect of peptide group-water interaction on β-structure conformation
1Kayava A. V., 1Lim V. I.
  1. Institute of Protein Research, Academy of Sciences of the USSR
    Pushchino, Moscow Region, USSR


An approach to estimate the effect of protein-solvent interactions on the polypeptide chain conformation is presented. The stereochemical analysis was based on the tendency of water molecules to form four hydrogen bonds with a tetrahedral orientation and was made with molecular models and computer calculations. It was shown that in the β-region of the conformational map the best polypeptide-water interaction takes place when the polypeptide chain has a polyproline conformation. We have shown that the right-handed twist of β-hairpins, determined by its intra- and interchain interactions, increases by virtue of the peptide group-water interaction. With an increase of the twist the most probable conformation of β-hairpins splits into two β-conformations, alternating along the β-strands. The β-structure conformation, predicted by our stereochemical analysis, agrees well with the β-structure conformations observed in globular proteins.


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