 I'm Wellenshi from Indiana University, and this is my advisor, Keith Stunker, and we are going to talk about our research, which is going to publish in Protein Science in March 2013. And the title of our paper is Exploring the Binding 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. And 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. Raylan will describe our strategy for finding these examples. Yes. Our rationale here is to search for the same protein segment bound to two or more partners in Protein Data Bank, and collect as many hot proteins as we can, and see how protein disorder facilitates hot proteins to associate with multiple partners. The sequence identities between partners should be less than 25 percent. And based on this 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, their backbone have relatively similar fold, but with low side-chain identity. There are 15 examples like this. On the other hand, there are eight examples in class two, and those proteins' backbone have completely different folds. So in the first class, we see we have five partners bound to one chain. This is actually the nuclear scepter one and two that have almost identical sequences, but they have the same binding motif. And what we've done in this figure is we've superimposed the backbones, and that leads to a superposition of the peptides bound to each protein. And in this 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-Len will talk about the second class. Yes. In our second class of hub proteins, as we can see in this diagram, the protein segments are from the end terminus of the histone three. As we can tell from the partner, the nine partners here, their conformation are totally different fold. 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.