Analyzing the value of the RMSD value calculated for all heavy atoms for the C.HSV peptide, it can be seen that its structure at the very beginning of the dynamics and between 300 and 600 ns of the dynamics was significantly different from the initial structure, but after 600 ns it was stabilized and did not change until the end of the MD (Figure ). Such changes in the structure of this peptide were also reflected in the Rg value increase during 300-600 ns (Figure ). It is clear that this peptide unfolded (hence higher RMSD values) and then folded again after 600 ns of dynamics and finally formed a helix. Final structure of the C.HSV peptide adopts a righthanded α-helical structure in the middle region (L62-A65). Backbone RMSD of the superposed structures to the average conformation was estimated to be 0.534Å (SD: 0.065Å) in the αhelical region (L62-A65) for the last 100ns of the simulation (Figure , Table ).