The interproton distances were calculated on the basis of the NOE intensities extracted from the NOESY spectra at a mixing time of 150 ms for N.HSV and C.HSV peptides. 470 and 300 distance restraints were provided for N.HSV and C.HSV, respectively. The initial structure of the peptide was calculated by a simulated annealing algorithm with distance restraints, which included 10000 steps of MD in the torsion angle space (CYANA software) . In the next stage, the peptide -DPC micelle system was created. Systems used in computational studies were created using Micelle Builder , included in CHARMM-GUI server . Simulation of N-and C-terminal parts of the HSV protein was started from conformations obtained by NMR inserted into micelles that consisted of 120 DPC molecules and surrounded by water molecules and Na + and Cl -ions to obtain ionic concentration of about 0.15M. Then minimization and equilibration simulations were run, completed by 1000ns of nvt productive run. Salt bridges were evaluated using ESBRI software . Hydrogen bonds were analyzed using the DSSP (Define Secondary Structure of Proteins) method implemented into the cpptraj program, a part of AMBER20 package.