But in the absence of the substrate molecule, when none of the active sites are filled by the substrate molecules, that means all the enzymes will predominate in the T state. Now, the thing about the Rstate is the r state describes this relaxed state, relaxed structure where there is not too much constraint and so definitive of the active side for the substrate is high and that represents a high catalytic activity, a high catalytic rate. Now, what we still haven't discussed is where the CTP actually binds to and how exactly does the binding of the CTP molecule to the regulatory dimer? That's where it binds to. How exactly is the binding of the CTP onto these regulatory dimers actually inhibits affects the activity of that enzyme? This is what we actually want to focus on in the next lecture and we're also going to discuss what this molecule or how this molecule actually exhibits the process of cooperativity.