Long molecular dynamics simulations of intrinsically disordered proteins reveal preformed structural elements for target binding

E.A. Cino, M.E.J. Karttunen, W.-Y. Choy

Research output: Chapter in Book/Report/Conference proceedingChapterAcademic

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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.
Original languageEnglish
Title of host publicationComputational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods
EditorsM. Fuxreiter
Place of PublicationBoca Raton
PublisherCRC Press
Chapter8
Pages233-256
ISBN (Electronic)9780429194689
ISBN (Print)978-1-4665-6157-1
Publication statusPublished - 2015
Externally publishedYes

Publication series

NameSeries in Computational Biophysics

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    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.