Investigating the role of large-scale domain dynamics in protein-protein interactions

Elise Delaforge; Sigrid Milles; Jie Rong Huang; Denis Bouvier; Malene Ringkjøbing Jensen; Michael Sattler; Darren J. Hart; Martin Blackledge

doi:10.3389/fmolb.2016.00054

Investigating the role of large-scale domain dynamics in protein-protein interactions

Elise Delaforge, Sigrid Milles, Jie Rong Huang, Denis Bouvier, Malene Ringkjøbing Jensen, Michael Sattler, Darren J. Hart, Martin Blackledge^*

^*此作品的通信作者

生化暨分子生物研究所

研究成果: Short survey › 同行評審

19 引文斯高帕斯（Scopus）

摘要

Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

原文	English
文章編號	54
期刊	Frontiers in Molecular Biosciences
卷	3
發行號	SEP
DOIs	https://doi.org/10.3389/fmolb.2016.00054
出版狀態	Published - 13 9月 2016

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abstract = "Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.",

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AU - Delaforge, Elise

AU - Milles, Sigrid

AU - Huang, Jie Rong

AU - Bouvier, Denis

AU - Jensen, Malene Ringkjøbing

AU - Sattler, Michael

AU - Hart, Darren J.

AU - Blackledge, Martin

PY - 2016/9/13

Y1 - 2016/9/13

N2 - Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

AB - Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

KW - Chemical exchange saturation transfer (CEST)

KW - Conformational dynamics

KW - Free-energy landscape

KW - Multi-domain proteins

KW - Nuclear magnetic resonance (NMR)

KW - Single molecule Förster resonance energy transfer (FRET)

KW - Small angle scattering

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M3 - Short survey

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SN - 2296-889X

VL - 3

JO - Frontiers in Molecular Biosciences

JF - Frontiers in Molecular Biosciences

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ER -

Investigating the role of large-scale domain dynamics in protein-protein interactions

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