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. Author manuscript; available in PMC: 2014 May 23.
Published in final edited form as: J Phys Chem B. 2013 May 15;117(20):6175–6186. doi: 10.1021/jp402938p

Figure 5.

Figure 5

Force curves acquired at 5 nm/ns pulling rate from SMD simulation. (a) Pulling the center of mass of Cys13 of monomer A (COM13A) along the z-axis. The central structure of the largest cluster of the last 50 ns of the MD simulation of the dimer is in a rectangular box. For clarity the water molecules are not shown. The dimension of the box is 6.555 nm × 4.376 nm × 18 nm. The pulling direction is indicated by a dashed arrow. Backbone conformation of the peptide chain is as follows: cyan is random meander; green is β-turn/bend, red arrow is β-sheet. Numbers inside the force curve panels indicate the time (b) and distance (c) locations of the characteristic peaks. Arrows and numbers on panel b indicate the snapshots in figure 6.