Once the practical ability of using classical MD to model hBChE is established, some intriguing directions may be pursued. Previously we suggested that conformational rearrangements of the acyl-binding loop explain the OPase activity of cl14 and cl15 variants. Quantitative evaluation of this idea with MD treatment may be beneficial in general and instrumental for other similar cases that recently emerged. Our results on the protonation prompt to re-evaluate possibilities for various proposed mechanisms of G117H action 7 that may potentially include minor conformations, unseen in x-ray, being the reactive ones. Being able to obtain ensembles of conformations also dramatically raises the possibilities of modern computational protein design approaches that may help to create a better OPase hBChE variant.