Maybe some naive question, but I need your opinion. I am doing research on docking to enzyme and it's mutants to show the change in Ki. The change in Ki is rather simple to show, but one thing is disturbing. I have 10 mutants and 10 Ki for each of 3 studied inhibitors. One of the mutant change the behavior of Ki of one inhibitor from nonlinear to linear. So, I stacked! I don't know the reason for change of this behavior because the amino acid is important for Ki - the change in it is 500 fold, but actually lay on the periphery of the binding site.
So, I need your opinion on this and some questions 1. Is is possible to show the change in nonlinear-linear change using protein-ligand complexes obtained by docking? 2. From enzyme structure only without docking?
