Related ArticlesUltra fast magic angle spinning solid - state NMR spectroscopy of intact bone.
Magn Reson Chem. 2016 Feb;54(2):132-5
Authors: Singh C, Rai RK, Kayastha AM, Sinha N
Abstract
Ultra fast magic angle spinning (MAS) has been a potent method to significantly average out homogeneous/inhomogeneous line broadening in solid-state nuclear magnetic resonance (ssNMR) spectroscopy. It has given a new direction to ssNMR spectroscopy with its different applications. We present here the first and foremost application of ultra fast MAS (~60 kHz) for ssNMR spectroscopy of intact bone. This methodology helps to comprehend and elucidate the organic content in the intact bone matrix with resolution and sensitivity enhancement. At this MAS speed, amino protons from organic part of intact bone start to appear in (1) H NMR spectra. The experimental protocol of ultra-high speed MAS for intact bone has been entailed with an additional insight achieved at 60 kHz.
[NMR paper] Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Related Articles Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
J Biomol NMR. 2016 Jan 19;
Authors: Wang S, Matsuda I, Long F, Ishii Y
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce...
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Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce the ambiguity for protein main-chain signal assignments in fast magic-angle-spinning (MAS) conditions at a wide frequency range of 40â??80Â*kHz. The approach termed HIGHLIGHT (Wang et al., in Chem Comm 51:15055â??15058, 2015) combines the reverse 13C,...
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[NMR paper] Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Related Articles Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.
Methods Mol Biol. 2016;1345:173-83
Authors: Tuttle MD, Courtney JM, Barclay AM, Rienstra CM
Abstract
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity...
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10-12-2015 01:04 AM
[NMR paper] A unified heteronuclear decoupling strategy for magic-angle-spinning solid-state NMR spectroscopy.
A unified heteronuclear decoupling strategy for magic-angle-spinning solid-state NMR spectroscopy.
Related Articles A unified heteronuclear decoupling strategy for magic-angle-spinning solid-state NMR spectroscopy.
J Chem Phys. 2015 May 14;142(18):184201
Authors: Equbal A, Bjerring M, Madhu PK, Nielsen NC
Abstract
A unified strategy of two-pulse based heteronuclear decoupling for solid-state magic-angle spinning nuclear magnetic resonance is presented. The analysis presented here shows that different decoupling sequences like...
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05-17-2015 03:52 PM
[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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04-11-2015 12:04 AM
[NMR paper] High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
Related Articles High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.
J Biomol NMR. 2013 Dec 13;
Authors: Ward ME, Wang S, Krishnamurthy S, Hutchins H, Fey M, Brown LS, Ladizhansky V
Abstract
Magic angle spinning nuclear magnetic resonance (MAS NMR) is well suited for the study of membrane proteins in membrane mimetic and native membrane...
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12-18-2013 04:00 PM
[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 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,...
Ultra fast magic angle spinning solid - state NMR spectroscopy of intact bone.
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