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. 2016 May 23;10(5):e0004710. doi: 10.1371/journal.pntd.0004710

Fig 3. Alteration in overall structure and the helicity of the peptide binding domain (PBD).

Fig 3

Panel A provides RMSD trajectories of the PBD extracted from the simulations with (dark grey) and without (light grey) the docked cholesterol. Panel B and C provide the plots where percentages of residues in α-helix conformation are plotted against the simulation time for chain A PBD helix (residues: 50–80) and Chain B PBD helix (residues: 52–89), respectively. White and black lines represent moving averages (period: 10) of the raw data.