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.
|Title of host publication||Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods|
|Place of Publication||Boca Raton|
|Publication status||Published - 2015|
|Name||Series in Computational Biophysics|
Cino, E. A., Karttunen, M. E. J., & Choy, W-Y. (2015). Long molecular dynamics simulations of intrinsically disordered proteins reveal preformed structural elements for target binding. In M. Fuxreiter (Ed.), Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods (pp. 233-256). (Series in Computational Biophysics). CRC Press.