NMR spectroscopy has been applied to virtually all sites within proteins and biomolecules; however, the observation of sulfur sites remains very challenging. Recent studies have examined ^(77)Se as a replacement for sulfur and applied ^(77)Se NMR in both the solution and solid states. As a spin-1/2 nuclide, ^(77)Se is attractive as a probe of sulfur sites, and it has a very large chemical shift range (due to a large chemical shift anisotropy), which makes it potentially very sensitive to...
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
Abstract
The robustness of NMR coherence transfer in proximity of a paramagnetic center depends on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins, different pulse schemes or different parameter sets often provide complementary results. Tailored versions of HCACO and CACO experiments significantly increase the number of observed Cα/Câ?? connectivities in highly paramagnetic systems, by recovering...
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10-19-2023 01:17 PM
[NMR paper] Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
Paramagnetic NMR to study iron sulfur proteins: 13C detected experiments illuminate the vicinity of the metal center
The robustness of NMR coherence transfer in proximity of a paramagnetic center depends on the relaxation properties of the nuclei involved. In the case of Iron-Sulfur Proteins, different pulse schemes or different parameter sets often provide complementary results. Tailored versions of HCACO and CACO experiments significantly increase the number of observed C^(?)/C' connectivities in highly paramagnetic systems, by recovering many resonances that were lost due to...
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10-19-2023 01:17 PM
77Se-13C based dipolar correlation experiments to map selenium sites in microcrystalline proteins
77Se-13C based dipolar correlation experiments to map selenium sites in microcrystalline proteins
Abstract
Sulfur-containing sites in proteins are of great importance for both protein structure and function, including enzymatic catalysis, signaling pathways, and recognition of ligands and protein partners. Selenium-77 is an NMR active spin-1/2 nucleus that shares many physiochemical properties with sulfur and can be readily introduced into proteins at sulfur sites without significant perturbations to the protein structure. The sulfur-containing...
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03-24-2022 02:19 PM
[NMR paper] NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
NMR Backbone Assignment of Large Proteins by Using (13) C? -Only Triple-Resonance Experiments.
Chemistry. 2016 Jun 8;
Authors: Wei Q, Chen J, Mi J, Zhang J, Ruan K, Wu J
Abstract
Nuclear magnetic resonance (NMR) is a powerful tool to interrogate protein structure and dynamics residue by residue. However, the prerequisite chemical-shift assignment remains a bottleneck for large proteins due to the fast relaxation and the frequency...
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06-09-2016 07:44 PM
[NMR paper] Detection of the water-binding sites of the oxygen-evolving complex of Photosystem II using W-band 17O electron-electron double resonance-detected NMR spectroscopy.
Detection of the water-binding sites of the oxygen-evolving complex of Photosystem II using W-band 17O electron-electron double resonance-detected NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Detection of the water-binding sites of the oxygen-evolving complex of Photosystem II using W-band 17O electron-electron double resonance-detected NMR spectroscopy.
J Am Chem Soc. 2012 Oct 10;134(40):16619-34
Authors: Rapatskiy L, Cox N, Savitsky A, Ames WM, Sander J,...
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03-02-2013 11:45 AM
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Three-dimensional triple-resonance NMR Spectroscopy of isotopically enriched proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 423-441</br>
Lewis E.*Kay, Mitsuhiko*Ikura, Rolf*Tschudin, Ad*Bax</br>
Four new and complementary three-dimensional triple-resonance experiments are described for obtaining complete backboneH,C, andN resonance assignments of proteins uniformly enriched withC andN. The new methods all rely onH detection and use multiple magnetization transfers through well-resolved one-bondJcouplings. Therefore, the...
[NMR paper] 77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase.
77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase.
Related Articles 77Se NMR characterization of 77Se-labeled ovine erythrocyte glutathione peroxidase.
J Biol Chem. 1991 Mar 15;266(8):4804-9
Authors: Gettins P, Crews BC
Lambs, maintained on a selenium-deficient diet supplemented with 94 atom % Na2 27SeO3, have been used as a source of 77Se-enriched erythrocyte glutathione peroxidase. After 5 months on this diet, the percentage of selenium in the enzyme derived from the supplement had reached 88%. From each...
Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR
Linear Mode
