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

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 proceeding › Chapter › Academic

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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 language	English
Title of host publication	Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods
Editors	M. Fuxreiter
Place of Publication	Boca Raton
Publisher	CRC Press
Chapter	8
Pages	233-256
ISBN (Electronic)	9780429194689
ISBN (Print)	978-1-4665-6157-1
Publication status	Published - 2015
Externally published	Yes

Publication series

Name	Series in Computational Biophysics

Cite this

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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",

}

Long molecular dynamics simulations of intrinsically disordered proteins reveal preformed structural elements for target binding. / Cino, E.A.; Karttunen, M.E.J.; Choy, W.-Y.
Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods. ed. / M. Fuxreiter. Boca Raton: CRC Press, 2015. p. 233-256 (Series in Computational Biophysics).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic

TY - CHAP

T1 - Long molecular dynamics simulations of intrinsically disordered proteins reveal preformed structural elements for target binding

AU - Cino, E.A.

AU - Karttunen, M.E.J.

AU - Choy, W.-Y.

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

M3 - Chapter

SN - 978-1-4665-6157-1

T3 - Series in Computational Biophysics

SP - 233

EP - 256

BT - Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods

A2 - Fuxreiter, M.

PB - CRC Press

CY - Boca Raton

ER -

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

Abstract

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