[Molecular dynamics of zervamicin II and its analogues in water and methanol].

A comparative study of the molecular dynamics of zervamicin II (an antimicrobial peptide from the peptaibol group, which has the channel-forming activity) in water and methanol has been performed. The influence of amino acid substitutions on the dynamics and stability of the peptide structure has been investigated. The amino acid sequence responsible for the absence of swivel motions in short peptaibols has been determined.

[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.