To better understand the slow motions of the protein in these complexes, we examined the structures at several time points of the simulations, and observed that the conformation of the C-terminal loops and helix changes significantly during the simulations. An example is provided in Figure , which depicts snapshots at 40 µs intervals (Figures ) during run A of the fV complex. This corresponds to the leftmost chart in Fig. . It is evident that the C-terminus gradually reconfigures from its initial, crystallographic conformation to a new conformation, in which the helix has rotated by about 90 degrees. Despite this rearrangement of the C-terminal components of the protein, the rest of the protein, including the binding site region, maintains a stable structure. This may be seen more clearly in Figure , which is an overlay of the structures of Figures , rotated so the binding site faces the viewer.