Prediction of interactions involving intrinsically disordered proteins

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Intrinsically disordered (ID) proteins play a central role in protein interactomes because their ID segments often mediate large numbers of interactions. We have shown previously that interactions mediated by ID protein segments are characterized by features that distinguish them from other protein interactions. We hypothesize that these features can be used to (i) identify interaction sites on globular proteins that preferentially bind ID proteins and (ii) determine the structures that ID protein segments adopt upon binding. Based on this hypothesis, we propose the following aims: