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Abstract
A quantum-chemical calculation procedure intended for studying geometries and electronic structures of various peptides was tested using the tetrapeptide Ala-Gly-Asp-Pro as example. The trajectory of the molecular dynamics of the Ala-Gly-Asp-Pro molecule in the surrounding of water molecules was followed for a period of 1500 ps. The conformation of the peptide molecule does not change within this period. The water surrounding of the Ala-Gly-Asp-Pro molecule prevents formation of an intramolecular salt bridge between the nitrogen atom of the terminal amino group and oxygen atoms of the side carboxy group of Asp. It is suggested that the mechanism of the physiological action of Ala-Gly-Asp-Pro may involve hydrogen bonding with one or several functional groups of this molecule.
Published Version
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