Biopolym. Cell. 1988; 4(2):79-85.
Structure and Function of Biopolymers
Effect of peptide group-water interaction on β-structure conformation
- Institute of Protein Research, Academy of Sciences of the USSR
Pushchino, Moscow Region, USSR
Abstract
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.
Full text: (PDF, in Russian)
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