Here we introduce a new pulse sequence for resonance assignment that halves the number of data sets required for sequential linking by directly correlating sequential amide resonances in a single diagonal-free spectrum. The method is demonstrated with both microcrystalline and sedimented deuterated proteins spinning at 60 and 111Â*kHz, and a fully protonated microcrystalline protein spinning at 111Â*kHz, with as little as 0.5Â*mg protein sample. We find that amide signals have a low chance of ambiguous linkage, which is further improved by linking in both forward and backward directions. The spectra obtained are amenable to automated resonance assignment using general-purpose software such as UNIO-MATCH.
[NMR paper] Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles Nano-Mole Scale Side-Chain Signal Assignment by 1H-Detected Protein Solid-State NMR by Ultra-Fast Magic-Angle Spinning and Stereo-Array Isotope Labeling.
PLoS One. 2015;10(4):e0122714
Authors: Wang S, Parthasarathy S, Nishiyama Y, Endo Y, Nemoto T, Yamauchi K, Asakura T,...
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Rapid Proton-DetectedNMR Assignment for Proteinswith Fast Magic Angle Spinning
Rapid Proton-DetectedNMR Assignment for Proteinswith Fast Magic Angle Spinning
Emeline Barbet-Massin, Andrew J. Pell, Joren S. Retel, Loren B. Andreas, Kristaps Jaudzems, W. Trent Franks, Andrew J. Nieuwkoop, Matthias Hiller, Victoria Higman, Paul Guerry, Andrea Bertarello, Michael J. Knight, Michele Felletti, Tanguy Le Marchand, Svetlana Kotelovica, Inara Akopjana, Kaspars Tars, Monica Stoppini, Vittorio Bellotti, Martino Bolognesi, Stefano Ricagno, James J. Chou, Robert G. Griffin, Hartmut Oschkinat, Anne Lesage, Lyndon Emsley, Torsten Herrmann and Guido Pintacuda
...
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[NMR paper] Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
Rapid proton-detected NMR assignment for proteins with fast magic angle spinning.
J Am Chem Soc. 2014 Aug 7;
Authors: Barbet-Massin E, Pell AJ, Retel J, Andreas LB, Jaudzems K, Franks WT, Nieuwkoop AJ, Hiller M, Higman VA, Guerry P, Bertarello A, Knight MJ, Felletti M, Le Marchand T, Kotelovica S, Akopjana I, Tars K, Stoppini M, Bellotti V, Bolognesi M, Ricagno S, Chou JJ, Griffin RG, Oschkinat H, Lesage A, Emsley L, Herrmann T, Pintacuda G
Abstract
...
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[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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Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination
Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination
Abstract Several techniques for spectral editing of 2D 13Câ??13C correlation NMR of proteins are introduced. They greatly reduce the spectral overlap for five common amino acid types, thus simplifying spectral assignment and conformational analysis. The carboxyl (COO) signals of glutamate and aspartate are selected by suppressing the overlapping amide Nâ??CO peaks through 13Câ??15N dipolar dephasing. The sidechain methine (CH) signals of valine,...
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[NMR paper] Probing membrane protein orientation and structure using fast magic-angle-spinning so
Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
Related Articles Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR.
J Biomol NMR. 2004 Nov;30(3):253-65
Authors: Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DT, Angerstein B, Luca S, Koert U, Killian JA, Baldus M
One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides...
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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,...
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[NMR paper] Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures wi
Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling.
Related Articles Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling.
J Am Chem Soc. 2004 Nov 17;126(45):14746-51
Authors: Etzkorn M, Böckmann A, Lange A, Baldus M
A general NMR strategy to directly study molecular interfaces under magic angle spinning is introduced. The approach is based on the spectroscopic analysis of uniformly, but heterogeneously, labeled...
Protein residue linking in a single spectrum for magic-angle spinning NMR assignment
Linear Mode
