[NMR paper] Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.
Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.
Related Articles Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.
Solid State Nucl Magn Reson. 2021 Jan 07;111:101710
Authors: Vugmeyster L
Abstract
Slow timescale dynamics in proteins are essential for a variety of biological functions spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as well as protein-protein and protein-nucleic acid interactions....
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01-16-2021 04:55 PM
[NMR paper] Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
Solid-state NMR provides evidence for small-amplitude slow domain motions in a multi-spanning transmembrane ?-helical protein.
J Am Chem Soc. 2017 Jun 14;
Authors: Good D, Pham C, Jagas J, Lewandowski JR, Ladizhansky V
Abstract
Proteins are dynamic entities and populate ensembles of conformations. Transitions between states within a conformational ensemble occur over a broad spectrum of amplitude...
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[NMR paper] Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
Ultraslow Domain Motions in HIV-1 TAR RNA Revealed by Solid-State Deuterium NMR.
J Phys Chem B. 2016 Dec 08;
Authors: Huang W, Emani PS, Varani G, Drobny GP
Abstract
Intrinsic motions may allow HIV-1 TAR RNA to change its conformation to form a functional complex with the Tat protein, which is essential for viral replication. Understanding the dynamic properties of TAR necessitates determining motion on the intermediate ns-?s time scale. To...
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[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
J Magn Reson. 2014 Sep 20;248C:8-12
Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K
Abstract
(15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms...
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[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation
Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation
Publication date: Available online 20 September 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Alexey Krushelnitsky , Tatiana Zinkevich , Bernd Reif , Kay Saalwächter</br>
15N NMR relaxation rate R 1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s - ms timescale range. On the basis of a comparison of 2D site-resolved with 1D integrated 15N...
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[NMR paper] NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
J Phys Chem B. 2013 May 2;
Authors: Xia J, Deng NJ, Levy RM
Abstract
Calculating NMR relaxation effects for proteins with dynamics on multiple timescales generally requires very long trajectories based on conventional molecular dynamics simulations. In this report,...
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins - ScienceDirect
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