@inbook{6f3a44ff58314301bc9f13556a144745,
title = "Long molecular dynamics simulations of intrinsically disordered proteins reveal preformed structural elements for target binding",
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.",
author = "E.A. Cino and M.E.J. Karttunen and W.-Y. Choy",
year = "2015",
language = "English",
isbn = "978-1-4665-6157-1",
series = "Series in Computational Biophysics",
publisher = "CRC Press",
pages = "233--256",
editor = "M. Fuxreiter",
booktitle = "Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods",
}