To this end, we concatenate six, 100 ns parallel trajectories each of benzene, butylbenzene and hexylbenzene bound to their native crystal structures to generate a concatenated trajectory totaling 1.8 µs. In this concatenated trajectory, we select all the C α -C α and C β -C β pairwise distances within the protein F-helix (residues 107-115) and apply TICA to resolve a set of tICs. We map all frames of the concatenated trajectory onto the top two tICs, thus projecting the data onto a two-dimensional (2D) TICA surface. We find that our 2D TICA surface consists of two primary regions of density -a larger half-moon region on the left and a smaller oval-shaped well on the right -with a bridge region connecting them (Figure ).