The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and hydrogen exchange. In this work, we demonstrate a protocol for multi-dimensional solid-state NMR spectral editing of signals from basic sidechains based on Hadamard matrix encoding. The Hadamard method acquires multi-dimensional experiments in such a way that both the backbone and under-sampled...
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
Abstract
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and hydrogen exchange. In this work, we demonstrate a protocol for multi-dimensional solid-state NMR spectral editing of signals from basic sidechains based on Hadamard matrix encoding. The Hadamard method acquires multi-dimensional experiments in such a...
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01-30-2025 03:23 PM
[NMR paper] Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and hydrogen exchange. In this work, we demonstrate a protocol for multi-dimensional solid-state NMR spectral editing of signals from basic sidechains based on Hadamard matrix encoding. The Hadamard method acquires multi-dimensional experiments in such a way that both the backbone and under-sampled...
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08-31-2024 01:47 PM
[NMR paper] Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing
Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing
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....
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09-10-2023 02:39 AM
[NMR paper] Structural dynamics of light harvesting proteins, photosynthetic membranes, and cells observed by spectral editing solid-state NMR
Structural dynamics of light harvesting proteins, photosynthetic membranes, and cells observed by spectral editing solid-state NMR
Photosynthetic light-harvesting complexes have a remarkable capacity to perform robust photo-physics at ambient temperatures and in fluctuating environments. Protein conformational dynamics and membrane mobility are processes that contribute to the light-harvesting efficiencies and control photoprotective responses. This short review describes the application of magic angle spinning nuclear magnetic resonance (NMR) spectroscopy for characterizing the structural...
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07-17-2022 10:07 PM
[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] 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 13Cā??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 Nā??CO peaks through 13Cā??15N dipolar dephasing. The sidechain methine (CH) signals of valine,...