For the N.HSV peptide, the RMSD values increased slowly over the time of the molecular dynamics (Figure ), which means that the peptide changed its structure in relation to its initial structure, but these changes are not very large. It is also visible in the analysis of Rg values that the peptide increases its radius of gyration, which means that it unfolds slowly or that its structure is flexible in MD time in relation to the initial structure (Figure ). The MD result shows that the final structure of the N.HSV (PDB code: XXXXX) adopts a righthanded α-helical structure in its middle region (P9-R15) whereas N-terminal residues (D1-P8)