I'm Wellen She from Indiana University and this is my advisor, Keith Duncan. We are going to talk about our research which is going to publish in protein science in March 2013. The title of our paper is, is, blurring the biting diversity of intrinsically disordered protein involved in one to many binding. So for many years people have discussed the importance of disordered proteins for binding to multiple partners and there have been a few examples published of the structures of such complexes but very few. Our goal here was to collect a much larger number of examples where the same peptide which was likely disordered in the unbound state is bound to multiple partners. Wellen will describe our strategy for finding these examples. Yes. Our rationale here is to search for sen protein segments bound to two or more partners in protein data bank and collect as many hot proteins as we can and see how protein disordered facilitate up proteins to associate with multiple partners. The sequence identities between partners should be less than 25% and best on list criteria we found 23 hubs with two to nine binding partners. They can be grouped into two classes. Although the partners in the first class have low sequence identities, layer backbone have relatively similar folds but with low-sidescent identity. Layer R15 is sample like this. On the other hand, layer R8 is samples in class 2 and low proteins backbone have completely different folds. So in the first class, we have five partners bound to one chain. This is actually the nuclear sector 1 and 2 that have almost identical sequences but they have the same binding motif. What we've done in this figure is we've superimposed the backbone and that leads to a superposition of the peptides bound to each protein. And in the superposition, we see that the five different peptides have very similar structures but substantial local differences. There are changes in the backbone torsional angles, there are changes in the side chain torsional angles. And these enable the same sequence to bind to the different shapes presented by these five different receptors. So Wei Lan will talk about the second class. Yes. In our second class of hot proteins, as we can see in this diagram, the protein segments are from the unterminess of the histone 3. As we can tell from the partner, the nipotenters here, layer confirmation are totally different folds. So therefore, this segment cannot be superimposed well just like the one showing in the center. So we encourage you to read our paper. We bring up a number of additional points that we didn't have time to discuss here, such as the fact that post translational modification plays an important role in partner selection by these intrinsically disordered proteins, as well as alternative splicing also plays an important role. And we encourage you to read our paper to find more about these additional items. Thank you very much.