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E to the change in entropy S, when an unstructured protein is bound and folded (transiently), is smaller than when a structured protein is bound ( G = H S). This concept may be debated, however, due to the relative order of the IDP vs. the dis-order of water upon IDP-partner binding in aqueous media. ii) An open structure gives an IDP the ability to bind to more than one partner and present dif
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Ena and facilitated by the conformational flexibility of the chain [131]. These and other atomistic modeling studies suggest the importance of the flexible conformation of the IDPs for interaction with mineral crystals and with collagen [133]. The best demonstration of the importance of IDPs function in the mineralization process comes from studies of animals and people in which IDP has been manip
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