 So you already saw these curves, but now we have a bit more experimental support for them. We have the energy that drops, we have the entropy that also drops mostly over a narrow regime, and we have the free energy that then ends up having some sort of barrier. Now what we now know is that when I'm moving from the multi-globular to the native state, we've now seen that in that case the barrier is going to be due to the entropy. It's an entropic barrier, it's a searching process, it's going to be slow. If I'm unfolding the protein on the other hand I also have a barrier, but in this case the barrier is going to be energetic in nature. Easy to fix, just raise the temperature and it will be faster. So do you see the difference? If it's an entropic barrier it's a searching process and if you increase the temperature you're just going to perturb the system. The lower the temperature is the faster it will go. Entropy or energy barrier on the other hand give it more energy, it's going to have an easier time getting over the energy barrier. So what I still haven't showed you that what we need to crack is that how high is this barrier and why is the barrier so surprisingly low compared to Leventhal's paradox assumption? And we're not quite there yet. We're going to need to find a way to connect this barrier to the nucleation condensation model in particular. And then I had this part that I flipped under the rug that those plots that I showed you they're called Arrhenius plots. Arrhenius plots when I plot ln k versus 1 over t. As I mentioned it's in particular for protein folding it's very difficult to split the folding from the unfolding part. What I really would like to do is can I can't I have a simple plot where I just measure how quickly the entire system relaxes so that is how quickly does it fold or unfold in total including processes in both directions. There is such a way but we're going to need to derive what those folding rates are.