A novel deuterium-excited and proton-detected quadruple-resonance three-dimensional (3D) ²H(?)c(?)NH MAS nuclear magnetic resonance (NMR) method is presented to obtain site-specific ²H(?) deuterium quadrupolar couplings from protein backbone, as an extension to the 2D version of the experiment reported earlier. Proton-detection results in high sensitivity compared to the heteronuclei detection methods. Utilizing four independent radiofrequency (RF) channels (quadruple-resonance), we managed to...
Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D 2Hâ??13Câ??1H MAS NMR spectroscopy
Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D 2Hâ??13Câ??1H MAS NMR spectroscopy
Abstract
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....
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01-09-2022 12:39 AM
[NMR paper] Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D (2)H-(13)C-(1)H MAS NMR spectroscopy
Site-specific protein methyl deuterium quadrupolar patterns by proton-detected 3D (2)H-(13)C-(1)H MAS NMR spectroscopy
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, ^(13)C and ^(15)N 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...
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01-09-2022 12:39 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] Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
Related Articles Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data.
J Biomol NMR. 2014 Sep 6;
Authors: Xiang S, Chevelkov V, Becker S, Lange A
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate /Ni with CAi/COi or CAi-1/COi-1. The resulting 4D spectra exhibit excellent...
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09-07-2014 12:36 PM
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Towards automatic protein backbone assignment using proton-detected 4D solid-state NMR data
Abstract
We introduce an efficient approach for sequential protein backbone assignment based on two complementary proton-detected 4D solid-state NMR experiments that correlate \( {\text{H}}_{{\text{i}}}^{{\text{N}}} \) /Ni with CAi/COi or CAiâ??1/COiâ??1. The resulting 4D spectra exhibit excellent sensitivity and resolution and are amenable to (semi-)automatic assignment...
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09-06-2014 07:41 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...
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08-03-2011 12:00 PM
[NMR paper] Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectro
Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
Related Articles Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Sep 22;126(37):11422-3
Authors: Giraud N, Böckmann A, Lesage A, Penin F, Blackledge M, Emsley L
Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a...
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11-24-2010 10:01 PM
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analy
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Related Articles Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Biochem Biophys Res Commun. 2010 Oct 11;
Authors: Shi P, Xi Z, Wang H, Shi C, Xiong Y, Tian C
SH3 is a ubiquitous domain mediating protein-protein interactions....
Site-specific protein backbone deuterium 2H? quadrupolar patterns by proton-detected quadruple-resonance 3D 2H?c?NH MAS NMR spectroscopy
Linear Mode
