Related ArticlesParamagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
Inorg Chem. 2017 May 24;
Authors: Bertarello A, Schubeis T, Fuccio C, Ravera E, Fragai M, Parigi G, Emsley L, Pintacuda G, Luchinat C
Abstract
We present the first solid-state NMR study of an iron-sulfur protein. The combined use of very fast (60 kHz) magic-angle spinning and tailored radiofrequency irradiation schemes allows the detection and the assignment of most of the (1)H and (13)C resonances of the oxidized high-potential iron-sulfur protein I from Ectothiorhodospira halophila (EhHiPIP I), including those in residues coordinating the Fe4S4 cluster. For these residues, contact shifts as large as 100 and 400 ppm for (1)H and (13)C resonances, respectively, were observed, which represent the most shifted solid-state NMR signals ever measured in metalloproteins. Interestingly, by targeting EhHiPIP I in a crystalline environment, we were able to capture distinct paramagnetic signatures from the two conformations present in the asymmetric unit. The magnetic properties of the system were verified by following the temperature dependence of the contact-shifted cysteine resonances.
PMID: 28537393 [PubMed - as supplied by publisher]
[NMR paper] Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.
Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.
Related Articles Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.
J Biomol NMR. 2017 Jan 24;:
Authors: Guo C, Hou G, Lu X, Polenova T
Abstract
REDOR-based experiments with simultaneous (1)H-(13)C and (1)H-(15)N dipolar dephasing are explored for investigating intermolecular protein-protein interfaces in complexes formed by a U-(13)C,(15)N-labeled protein and its natural abundance...
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Mapping proteinâ??protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy
Mapping proteinâ??protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy
Abstract
REDOR-based experiments with simultaneous 1Hâ??13C and 1Hâ??15N dipolar dephasing are explored for investigating intermolecular proteinâ??protein interfaces in complexes formed by a Uâ??13C,15N-labeled protein and its natural abundance binding partner. The application of a double-REDOR filter (dREDOR) results in a complete dephasing of proton magnetization in the Uâ??13C,15N-enriched molecule while the proton magnetization of the unlabeled...
[NMR paper] Sensitivity and Resolution Enhanced Solid-State NMR for Paramagnetic Systems and Biomolecules under Very Fast Magic Angle Spinning.
Sensitivity and Resolution Enhanced Solid-State NMR for Paramagnetic Systems and Biomolecules under Very Fast Magic Angle Spinning.
Related Articles Sensitivity and Resolution Enhanced Solid-State NMR for Paramagnetic Systems and Biomolecules under Very Fast Magic Angle Spinning.
Acc Chem Res. 2013 Jul 26;
Authors: Parthasarathy S, Nishiyama Y, Ishii Y
Abstract
Recent research in fast magic angle spinning (MAS) methods has drasticallyimproved the resolution and sensitivity of NMR spectroscopy of biomolecules and materials in solids. In...
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07-31-2013 12:00 PM
[NMR paper] Magic Angle Spinning NMR of Paramagnetic Proteins.
Magic Angle Spinning NMR of Paramagnetic Proteins.
Related Articles Magic Angle Spinning NMR of Paramagnetic Proteins.
Acc Chem Res. 2013 Mar 18;
Authors: Knight MJ, Felli IC, Pierattelli R, Emsley L, Pintacuda G
Abstract
Metal ions are ubiquitous in biochemical and cellular processes. Since many metal ions are paramagnetic due to the presence of unpaired electrons, paramagnetic molecules are an important class of targets for research in structural biology and related fields. Today, NMR spectroscopy plays a central role in the...
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03-20-2013 01:47 PM
[NMR paper] Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Probing Structure and Dynamics of Protein Assemblies by Magic Angle Spinning NMR Spectroscopy.
Acc Chem Res. 2013 Feb 13;
Authors: Yan S, Suiter CL, Hou G, Zhang H, Polenova T
Abstract
In living organisms, biological molecules often organize into multicomponent complexes. Such assemblies consist of various proteins and carry out essential functions, ranging from cell division, transport, and energy transduction to catalysis, signaling, and viral...
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02-14-2013 02:37 PM
[NMR paper] Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Related Articles Magic angle spinning nuclear magnetic resonance spectroscopy of g protein-coupled receptors.
Methods Enzymol. 2013;522:365-89
Authors: Goncalves J, Eilers M, South K, Opefi CA, Laissue P, Reeves PJ, Smith SO
Abstract
G protein-coupled receptors (GPCRs) represent the largest family of membrane receptors and mediate a diversity of cellular processes. These receptors have a common seven-transmembrane helix structure, yet have evolved...
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[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
Related Articles Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
Paramagnetic Properties of a Crystalline Iron-Sulfur Protein by Magic-Angle Spinning NMR Spectroscopy.
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