ReviewProgress in nuclear magnetic resonance spectroscopy2013
Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins.
Review in Progress in nuclear magnetic resonance spectroscopy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Article
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
- Simultaneous recording of intra- and inter-residue linking experiments for backbone assignments in proteins at MAS frequencies higher than 60 kHz.Journal of biomolecular NMR · 2020Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Improving the quality of oriented membrane protein spectra using heat-compensated separated local field experiments.Journal of biomolecular NMR · 2019Article
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- Probing Residue-Specific Water-Protein Interactions in Oriented Lipid Membranes via Solid-State NMR Spectroscopy.The journal of physical chemistry. B · 2016Article
- Orphan spin polarization: A catalyst for high-throughput solid-state NMR spectroscopy of proteins.Annual reports on NMR spectroscopy · 2016Article
- Spatial reorientation experiments for NMR of solids and partially oriented liquids.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples.Journal of biomolecular NMR · 2015Article
- Action of the multifunctional peptide BP100 on native biomembranes examined by solid-state NMR.Journal of biomolecular NMR · 2015Article
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
- Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2015Article
- NMR-based detection of hydrogen/deuterium exchange in liposome-embedded membrane proteins.PloS one · 2014Article
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3 authors.
Funding
Abstract
Oriented solid-state NMR (O-ssNMR) spectroscopy is a major technique for the high-resolution analysis of the structure and topology of transmembrane proteins in native-like environments. Unlike magic angle spinning (MAS) techniques, O-ssNMR spectroscopy requires membrane protein preparations that are uniformly oriented (mechanically or magnetically) so that anisotropic NMR parameters, such as dipolar and chemical shift interactions, can be measured to determine structure and orientation of membrane proteins in lipid bilayers. Traditional sample preparations involving mechanically aligned lipids often result in short relaxation times which broaden the (15)N resonances and encumber the manipulation of nuclear spin coherences. The introduction of lipid bicelles as membrane mimicking systems has changed this scenario, and the more favorable relaxation properties of membrane protein (15)N and (13)C resonances make it possible to develop new, more elaborate pulse sequences for higher spectral resolution and sensitivity. Here, we describe our recent progress in the optimization of O-ssNMR pulse sequences. We explain the theory behind these experiments, demonstrate their application to small and medium size proteins, and describe the technical details for setting up these new experiments on the new generation of NMR spectrometers.
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