Solid-state NMR (ss-NMR) is a powerful tool to investigate noncrystallizable, poorly soluble molecular systems, such as membrane proteins, amyloids, and cell walls, in environments that closely resemble their physical sites of action. Rotational-echo double resonance (REDOR) is an ss-NMR methodology, which by reintroducing heteronuclear dipolar coupling under magic angle spinning conditions provides intramolecular and intermolecular distance restraints at the atomic level. In addition, REDOR can...
[NMR paper] Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Related Articles Hidden motions and motion-induced invisibility: dynamics-based spectral editing in solid-state NMR.
Methods. 2018 Apr 24;:
Authors: Matlahov I, van der Wel PCA
Abstract
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural characterization of a diverse array of biological assemblies that include amyloid fibrils, non-amyloid aggregates, membrane-associated proteins and viral capsids....
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04-28-2018 03:16 PM
[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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01-20-2016 11:54 PM
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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01-19-2016 07:37 PM
[NMR paper] Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Aromatic spectral editing techniques for magic-angle-spinning solid-state NMR spectroscopy of uniformly (13)C-labeled proteins.
Solid State Nucl Magn Reson. 2015 Sep 14;
Authors: Williams JK, Schmidt-Rohr K, Hong M
Abstract
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, have strongly overlapping (13)C chemical shift ranges between 100 and 160ppm,...
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10-07-2015 11:27 AM
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Publication date: Available online 14 September 2015
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Jonathan K. Williams, Klaus Schmidt-Rohr, Mei Hong</br>
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped 13C chemical shifts between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet...
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09-14-2015 10:42 PM
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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10-13-2012 04:42 AM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...
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08-22-2010 03:31 PM
[NMR paper] Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemota
Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor.
Biochemistry. 1997 Feb 18;36(7):1699-703
Authors: Wang J, Balazs YS, Thompson LK
The Escherichia coli serine receptor senses serine levels in the environment and transmits this information across the bacterial inner membrane to...