Abstract
Variation of the geometric parameters of a molecule of Epitalon tetrapeptide (Ala-Glu-Asp-Gly) over a period of 1500 ps was simulated by the method of molecular dynamics using AMBER force field. The structure of the molecule is stabilized by two salt bridges formed by the N-terminal nitrogen atom and oxygen atoms of Asp and Glu side chains. The biological effect of Epitalon was attributed to formation of salt or hydrogen bonds involving one or several ionizable functional groups of the molecules.
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