Now, the final question I'd like to explore is what did scientists actually see when that polymer molecule was bound onto the active side? What types of structural changes actually took place in the queen every structure of this atcase allosteric enzyme? Well, just like as we discussed in hemoglobin, when the oxygen molecules are not bound to the heme groups of hemoglobin, that hemoglobin molecule exists in the T state, in the ten state. And what that means is the entire coronary structure is constrained. And so the affinity of the heme groups for oxygen is very low. And in the same analogous way, because this allosteric enzyme basically exhibits cooperativity.