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 dynamics and longer-range tumbling of one or more peptide planes. This model provides unique insight into segmental organization of dynamics in IDPs and allows us to investigate the presence and extent of the correlated motions that are essential for function.
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] NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins.
NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins.
NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins.
Phys Chem Chem Phys. 2017 Apr 11;:
Authors: Kurzbach D, Beier A, Vanas A, Flamm AG, Platzer G, Schwarz TC, Konrat R
Abstract
A novel statistical analysis of paramagnetic relaxation enhancement (PRE) and paramagnetic relaxation interference (PRI) based nuclear magnetic resonance (NMR) data is proposed based on the...
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04-12-2017 10:57 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...
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06-15-2016 11:12 PM
[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...
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03-21-2014 12:52 AM
[NMR paper] Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.
Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.
Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.
Angew Chem Int Ed Engl. 2013 Mar 20;
Authors: Stanek J, Saxena S, Geist L, Konrat R, Ko?mi?ski W
Abstract
Ab ultra-high-resolution NMR experiment for the measurement of intraresidue (1) H(i)-(15) N(i)-(13) C'(i) dipolar-chemical shift anisotropy relaxation interference is employed to extract information about local backbone...
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03-23-2013 06:36 PM
[NMR paper] Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.
Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Fast hydrogen exchange affects (15)N relaxation measurements in intrinsically disordered proteins.
J Biomol NMR. 2013 Jan 12;
Authors: Kim S, Wu KP, Baum J
Abstract
Unprotected amide protons can undergo fast hydrogen exchange (HX) with protons from the solvent. Generally, NMR experiments using the out-and-back...
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02-03-2013 10:22 AM
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins
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