ABSTRACT
IDPs comprise >30% of the eukaryotic proteome [3,18,19]. e abundance of IDPs in organisms suggests that they are essential for numerous functions. Indeed, IDPs are found to be involved in crucial signaling and regulatory functions in cells [20-24]. e structural and dynamic properties of IDPs are well suited to their roles in signaling pathways, where reversible binding and the ability to interact with multiple partners are essential [1,4,6]. Clearly, IDPs are a biologically functional class of proteins that perform important functions while not conforming to the traditional structure-function paradigm.
