Determination of protein structure and dynamics is key to understand the mechanism of protein action. Perdeuterated proteins have been used to obtain high resolution/sensitivty NMR experiments via proton-detection. These methods utilizes 1H, 13C and 15N nuclei for chemical shift dispersion or relaxation probes, despite the existing abundant deuterons. However, a high-sensitivity NMR method to utilize deuterons and e.g. determine site-specific deuterium quadrupolar pattern information has been lacking due to technical difficulties associated with deuteriumâ??s large quadrupolar couplings. Here, we present a novel deuterium-excited and proton-detected three-dimensional 2Hâ??13Câ??1H MAS NMR experiment to utilize deuterons and to obtain site-specific methyl 2H quadrupolar patterns on detuterated proteins for the first time. A high-resolution fingerprint 1Hâ??15N HSQC-spectrum is correlated with the anisotropic deuterium quadrupolar tensor in the third dimension. Results from a model perdeuterated protein has been shown.
Off-resonance 13Câ??2H REDOR NMR for site-resolved studies of molecular motion
Off-resonance 13Câ??2H REDOR NMR for site-resolved studies of molecular motion
Abstract
We introduce a 13Câ??2H Rotational Echo DOuble Resonance (REDOR) technique that uses the difference between on-resonance and off-resonance 2H irradiation to detect dynamic segments in deuterated molecules. By selectively inverting specific regions of the 2H magic-angle spinning (MAS) sideband manifold to recouple some of the deuterons to nearby carbons, we distinguish dynamic and rigid residues in 1D and 2D 13C spectra. We demonstrate this approach on deuterated...
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08-03-2021 06:17 PM
[NMR paper] Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Related Articles Deuterium solid-state NMR quadrupolar order rotating frame relaxation with applications to amyloid-? fibrils.
Magn Reson Chem. 2020 Nov 08;:
Authors: Vugmeyster L, Ostrovsky D
Abstract
We describe a new method for measuring molecular dynamics based on the deuterium solid-state nuclear magnetic resonance (NMR) quadrupolar order rotating frame relaxation rate R1?,Q under static conditions. The observed...
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11-11-2020 09:42 AM
[NMR paper] Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Related Articles Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Chemphyschem. 2018 Jun 19;:
Authors: Zinke M, Fricke P, Lange S, Zinn-Justin S, Lange A
Abstract
Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no...
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06-20-2018 08:56 PM
[NMR paper] Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Related Articles Enhanced Spectral Density Mapping through Combined Multiple-Field Deuterium mCH2D Methyl Spin Relaxation NMR Spectroscopy.
Methods. 2017 Dec 27;:
Authors: Hsu A, O'Brien PA, Bhattacharya S, Rance M, Palmer AG
Abstract
Quadrupolar relaxation of 2H (D) nuclear spins is a powerful probe of conformational dynamics in biological macromolecules. Deuterium relaxation rate constants are determined by...
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01-01-2018 02:17 AM
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy
Abstract
Several amyloid fibrils have cores framed by highly dynamic, intrinsically disordered, domains that can play important roles for function and toxicity. To study these domains in detail using solid-state NMR spectroscopy, site-specific resonance assignments are required. Although the rapid dynamics of these domains lead to considerable averaging of orientation-dependent NMR interactions and thereby line-narrowing, the proton...
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11-19-2016 08:35 PM
[NMR paper] Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3
Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA
Abstract
At the...
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06-12-2013 11:42 AM
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Abstract Methyl-transverse relaxation optimized spectroscopy is rapidly becoming the preferred NMR technique for probing structure and dynamics of very large proteins up to ~1 MDa in molecular size. Data interpretation, however, necessitates assignment of methyl groups which still presents a very challenging and time-consuming process. Here we demonstrate that, in combination with a known 3D structure, paramagnetic...
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09-26-2011 06:42 AM
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...
Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D 2Hâ??13Câ??1H MAS NMR spectroscopy
Linear Mode
