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Keywords
Intrinsically disordered proteins; Folding funnel; Protein binding; Coupled folding and binding; Conformational selection
Introduction
One of the most intriguing features of IDPs is their ability to undergo disorder-to-order transitions upon binding in order to perform their function [13], [14] and [15]. Binding of IDPs offers unique advantages in cellular signaling and regulation. For instance, the ability of IDPs to be molded by their binding partner ensures that PR-957 binding to multiple targets will proceed selectively and with optimized binding rates. While there is Devonian a consensus opinion on the importance of intermolecular interactions involving IDPs, views on the possible mechanisms of binding are still divergent. Among the emerging mechanistic theories of IDP binding, two diametrically opposite models have been proposed: the ‘conformational selection’ and the ‘coupled folding and binding’. Both mechanistic models will be discussed in the following sections.
Conformational selection