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

Onderzoeksoutput: Hoofdstuk in Boek/Rapport/Congresprocedure › Hoofdstuk › Academic

4 Downloads (Pure)

Samenvatting

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.

Originele taal-2	Engels
Titel	Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods
Redacteuren	M. Fuxreiter
Plaats van productie	Boca Raton
Uitgeverij	CRC Press
Hoofdstuk	8
Pagina's	233-256
ISBN van elektronische versie	9780429194689
ISBN van geprinte versie	978-1-4665-6157-1
Status	Gepubliceerd - 2015
Extern gepubliceerd	Ja

Publicatie series

Naam	Series in Computational Biophysics

Citeer dit

@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",

}

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. redactie / M. Fuxreiter. Boca Raton: CRC Press, 2015. blz. 233-256 (Series in Computational Biophysics).

Onderzoeksoutput: Hoofdstuk in Boek/Rapport/Congresprocedure › Hoofdstuk › 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

Samenvatting

Publicatie series

Vingerafdruk

Citeer dit