and C-terminal (D16-G35) exhibit unordered structure (Figure ). The α-helical structure of N.HSV is stabilized by hydrogen bonds between the atoms of residues i,i+4: CO P9 -HN E11 , CO E11 -HN R15 , and CO G13 -HN G17 . These interactions are confirmed by medium-range NOE effects (such as αH-NH(i,i+3), αH-βH(i,i+3), and αH-NH(i,i+4)) in the P9-R15 region. This structure is stabilized by the salt bridges between residues E11-R15, E12-R15, E12-R22, D16-R22 (Figure ). Backbone RMSD of the superposed structures to the average conformation was estimated to be 0.457Å (SD: 0.179Å) in the α-helical region (P9-R15) for the last 100ns of the simulation (Figure , Table ). The C.HSV peptide moved fully out of the DPC micelle after about 20 ns of MD (Figure ). It is worth highlighting that this peptide alternately penetrated into or emerged from the micelles between 100 and 700 ns. Only after 700 ns of molecular dynamics, it stabilized its position on the micelle surface. The structural analysis showed that the Q60 and H67 residues were exposed to water (Figure ), while the R61-G66 fragment was located at the micellar surface and mostly interacted with the hydrophilic heads of the DPC molecules (Table ).