Abstract
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behaviour of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for understanding fundamental biological processes, the molecular basis of their activity still remains largely unknown. The functional mechanisms exploited by IDPs in their interactions with other biomolecules are defined by their intrinsic dynamic modes and associated timescales, justifying the considerable interest over recent years in the development of technologies adapted to measure and describe this behaviour. NMR spin relaxation delivers information-rich, site-specific data reporting on conformational fluctuations occurring throughout the molecule. Here we review recent progress in the use of (15)N relaxation to identify local backbone dynamics and long-range chain-like motions in unfolded proteins.
[NMR paper] Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Related Articles Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Angew Chem Int Ed Engl. 2017 Aug 22;:
Authors: Blackledge M, Salvi N, Abyzov A
Abstract
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly...
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08-25-2017 04:11 AM
[NMR paper] Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly flexible proteins, the absence of physical models describing IDP dynamics hinders their mechanistic interpretation. Combining molecular dynamics simulation and NMR, we introduce a framework in which distinct motions are attributed to local libration, backbone dihedral angle...
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08-23-2017 03:18 AM
Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation
Atomic Resolution Conformational Dynamics of Intrinsically Disordered Proteins from NMR Spin Relaxation
Publication date: Available online 10 July 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Nicola Salvi, Anton Abyzov, Martin Blackledge</br>
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behavior of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for...
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07-11-2017 09:20 AM
[NMR paper] Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
Related Articles Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation.
J Phys Chem Lett. 2016 Jun 14;
Authors: Salvi N, Abyzov A, Blackledge M
Abstract
Intrinsically disordered proteins (IDPs) access highly diverse ensembles of conformations in their functional states. Although this plasticity is essential to their function, little is known about the dynamics underlying...
[NMR paper] Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering.
Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering.
Related Articles Predictive Atomic Resolution Descriptions of Intrinsically Disordered hTau40 and ?-Synuclein in Solution from NMR and Small Angle Scattering.
Structure. 2013 Dec 18;
Authors: Schwalbe M, Ozenne V, Bibow S, Jaremko M, Jaremko L, Gajda M, Jensen MR, Biernat J, Becker S, Mandelkow E, Zweckstetter M, Blackledge M
Abstract
The development of molecular descriptions of intrinsically...
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12-24-2013 01:04 PM
[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR.
Describing intrinsically disordered proteins at atomic resolution by NMR.
Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR.
Curr Opin Struct Biol. 2013 Mar 29;
Authors: Jensen MR, Ruigrok RW, Blackledge M
Abstract
There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...
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04-03-2013 08:22 PM
Describing intrinsically disordered proteins at atomic resolution by NMR
Describing intrinsically disordered proteins at atomic resolution by NMR
Available online 29 March 2013
Publication year: 2013
Source:Current Opinion in Structural Biology</br>
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There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
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