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Off-resonance 13C??2H REDOR NMR for site-resolved studies of molecular motion
Aug 03, 2021 - 6:17 PM - by nmrlearner
nmrlearner's Avatar Off-resonance 13C??2H REDOR NMR for site-resolved studies of molecular motion

Abstract

We introduce a 13C??2H Rotational Echo DOuble Resonance (REDOR) technique that uses the difference between on-resonance and off-resonance 2H irradiation to detect dynamic segments in deuterated molecules. By selectively inverting specific regions of the 2H magic-angle spinning (MAS) sideband manifold to recouple some of the deuterons to nearby carbons, we distinguish dynamic and rigid residues in 1D and 2D 13C spectra. We demonstrate this approach on deuterated GB1, H/D exchanged GB1, and perdeuterated bacterial cellulose. Numerical simulations reproduce the measured mixing-time and 2H carrier-frequency dependence of the REDOR dephasing of bacterial cellulose. Combining numerical simulations with experiments thus allow the extraction of motionally averaged quadrupolar couplings from REDOR dephasing values.



Source: Journal of Biomolecular NMR
0 Replies | 1 Views
[NMR paper] Off-resonance (13)C-(2)H REDOR NMR for site-resolved studies of molecular motion
Aug 03, 2021 - 6:17 PM - by nmrlearner
nmrlearner's Avatar Off-resonance (13)C-(2)H REDOR NMR for site-resolved studies of molecular motion

We introduce a ^(13)C-H Rotational Echo DOuble Resonance (REDOR) technique that uses the difference between on-resonance and off-resonance H irradiation to detect dynamic segments in deuterated molecules. By selectively inverting specific regions of the H magic-angle spinning (MAS) sideband manifold to recouple some of the deuterons to nearby carbons, we distinguish dynamic and rigid residues in 1D and 2D ^(13)C spectra. We demonstrate this approach on deuterated GB1, H/D exchanged GB1, and...

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0 Replies | 1 Views
An automated iterative approach for protein structure refinement using pseudocontact shifts
Aug 02, 2021 - 5:20 PM - by nmrlearner
nmrlearner's Avatar An automated iterative approach for protein structure refinement using pseudocontact shifts

Abstract

NMR structure calculation using NOE-derived distance restraints requires a considerable number of assignments of both backbone and sidechains resonances, often difficult or impossible to get for large or complex proteins. Pseudocontact shifts (PCSs) also play a well-established role in NMR protein structure calculation, usually to augment existing structural, mostly NOE-derived, information. Existing refinement protocols using PCSs usually either require a sizeable number of sidechain assignments or are complemented by other experimental restraints. Here, we present an automated iterative procedure to perform backbone protein structure refinements requiring only a limited amount of backbone amide PCSs. Already known structural features from a starting homology model, in this case modules of repeat proteins, are framed into a scaffold that is subsequently refined by experimental PCSs. The method produces reliable indicators that can be monitored to judge about the performance. We applied it to a system in which sidechain assignments are hardly possible, designed Armadillo repeat proteins (dArmRPs), and we calculated the solution NMR structure of YM4A, a dArmRP containing four sequence-identical internal modules, obtaining high convergence to a single structure. We suggest that this approach is particularly useful when approximate folds are known from other techniques, such as X-ray crystallography, while avoiding inherent artefacts due to, for instance, crystal packing.



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0 Replies | 18 Views
Engineering Biologics toward Challenging Membrane Protein Targets - Genetic Engineering & Biotechnology News
Aug 02, 2021 - 5:20 PM - by nmrlearner
nmrlearner's Avatar Engineering Biologics toward Challenging Membrane Protein Targets Genetic Engineering & Biotechnology News
Engineering Biologics toward Challenging Membrane Protein Targets - Genetic Engineering & Biotechnology News
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0 Replies | 6 Views
Researchers discover titanium oxide nanoparticle that recognizes SARS-CoV-2s non-structural protein 1 - News-Medical.Net
Aug 02, 2021 - 5:20 PM - by nmrlearner
nmrlearner's Avatar Researchers discover titanium oxide nanoparticle that recognizes SARS-CoV-2s non-structural protein 1 - News-Medical.Net

Researchers discover titanium oxide nanoparticle that recognizes SARS-CoV-2s non-structural protein 1 News-Medical.Net Read here
0 Replies | 6 Views
Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User - GlobeNewswire
Aug 02, 2021 - 5:20 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User - GlobeNewswire

Protein Crystallization & Crystallography Market Research Report by Technology, by Product & Service, by End User GlobeNewswire Read here
0 Replies | 6 Views
[NMR paper] Structure and Dynamics Perturbations in Ubiquitin Adsorbed or Entrapped in Silica Materials Are Related to Disparate Surface Chemistries Resolved by Solid-State NMR Spectroscopy
Aug 02, 2021 - 5:20 PM - by nmrlearner
nmrlearner's Avatar Structure and Dynamics Perturbations in Ubiquitin Adsorbed or Entrapped in Silica Materials Are Related to Disparate Surface Chemistries Resolved by Solid-State NMR Spectroscopy

Protein immobilization on material surfaces is emerging as a powerful tool in the design of devices and active materials for biomedical and pharmaceutical applications as well as for catalysis. Preservation of the protein's biological functionality is crucial to the design process and is dependent on the ability to maintain its structural and dynamical integrity while removed from the natural surroundings. The scientific techniques to validate the structure of immobilized proteins are scarce and...

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0 Replies | 11 Views
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