Steered molecular dynamics simulations reveal critical residues for (un)binding of substrates, inhibitors and a product to the malarial M1 aminopeptidase
Table 1
Fluctuation of the radius of gyration (Rgyr) at several locations of the C- and N-terminal channels (see Fig 1) in the cMD simulations of the empty PfM1-AAP and during the ligand passage in the 100ns sMD simulations.