Kinetics of Bovine leukemia virus aspartic protease reveals its dimerization and conformational change
Fig 7
Confirmation of the plausibility of Scheme 3 through comparison between experimental and simulated data.
(A) Dependence of experimental (triangles) and simulated (circles) kobs on the concentration of the CA-NC substrate. The experimental values were obtained as in Fig 4 and represent the mean ± standard error (n = 4). The simulated data were obtained from numerical simulations using Scheme 3 and the rate constants obtained from time course experiments. The black traces represents the best fit of Eq 3. (B) Dependence of the experimental (triangles) and simulated (circles) steady state rate v on the concentration of the CA-NC substrate. The experimental values were obtained as in Fig 5 and represent the mean ± standard error (n = 4). The simulated data were obtained from numerical simulations as in (A). The black traces represents the best fit of the Michaelis-Menten equation.