[Molecular dynamics of oligopeptides. A comparative study of the interactions of amino acid residues in dipeptide structures].

A comparative study of the molecular dynamics of dipeptides consisting of natural amino acid residues has been carried out. Molecular dynamics protocols were used that do not violate the principle of equidistribution of energy by degrees of freedom. Autocorrelation functions of complex exponential curves from dihedrals were used for the comparative analysis. The interactions of amino acid residues were classified by their influence on the dynamic properties of neighboring amino acid residues.

[A molecular dynamics simulation study of human alpha-fetoprotein-derived peptide and its analogues. Influence of dielectric constant].

A comparative study of the conformation dynamics of a series of heptapeptides: the human alpha-fetoprotein fragment LDSYQCT and its seven analogues has been conducted. The effect of the dielectric constant of medium on the dynamics of heptapeptide conformation is considered. It is shown that electrostatic interactions have a marked effect on several accessible conformations and the dynamics of the behavior of amino acid residues.

[Molecular dynamics of oligopeptides 6. A comparative study of poincare cross-section of monopeptide frames in media with different hydrophobicity].

A comparative study of the molecular dynamics of natural amino acid residues and their closest homologues and isomers was carried out. Molecular dynamics protocols not interfering with the principle of equidistribution of energy with respect to degrees of freedom were used. Poincare cross-sections, auto- and cross-correlation of complex exponential curves as a function of dihedrons were considered. The classification of dynamic properties of conformational degrees of freedom in the series of amino acid residues was carried out.