3.4.23.16 specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro flap closing and conformational change mechanism induced by substrate binding in HIV-1 aspartic protease, flap conformations in the active site during the catalytic cycle, molecular dynamic simulations, overview 664137 3.4.23.16 specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro proteolysis mechanism whereby only one active site Asp is initially protonated. The steps of this mechanism are: asymmetric binding of the substrate, hydration of the peptidic carbonyl by an active site water, proton translocation between the active site Asp residue simultaneously with carbonyl hydration 648146 3.4.23.16 specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro the active site structure and conformational flexibility 666873 3.4.23.16 specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro the kinetic mechanism of HIV-1 protease is random, in which products bind to form both binary and ternary enzyme-product complexes, depending on the substrate used 648124