[NMR paper] Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.
Prog Nucl Magn Reson Spectrosc. 2017 Nov;102-103:43-60
Authors: Salvi N, Abyzov A, Blackledge M
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...
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11-22-2017 02:01 PM
[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] NMR contributions to structural dynamics studies of intrinsically disordered proteins.
NMR contributions to structural dynamics studies of intrinsically disordered proteins.
Related Articles NMR contributions to structural dynamics studies of intrinsically disordered proteins.
J Magn Reson. 2014 Apr;241:74-85
Authors: Konrat R
Abstract
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic...
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03-25-2014 11:49 AM
NMR contributions to structural dynamics studies of intrinsically disordered proteins
NMR contributions to structural dynamics studies of intrinsically disordered proteins
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): Robert Konrat</br>
Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development...