Figure 4
Dynamic changes of the secondary structure of a 150 residue vasoinhibin (Vi). (a) Changes of the secondary structure along the residue sequence of PRL (left) and the Vi (right) during 20 ns of molecular dynamic simulation (MD). The colours represent different secondary structures averaged from 3 independent MD. (b) Time percentage in helix conformation (helicity) per residue of PRL (black line) and Vi (red line) during a 200 ns MD simulation. Major discrepancies between PRL and Vi are indicated (*). (c) Free energy (DG) landscape (FEL) analysis of the Vi sampled throughout 200 ns of MD simulation. (d) Lowest energy structure obtained from FEL analysis.
