ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2020
De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy.JACS Au · 2023Article
- Extensively sparseJournal of biomolecular NMR · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane proteins perform many important cellular functions. Historically, structural studies of these proteins have been conducted in detergent preparations and synthetic lipid bilayers. More recently, magic-angle-spinning (MAS) solid-state NMR has been employed to analyze membrane proteins in native membrane environments, but resonance assignments with this technique remain challenging due to limited spectral resolution and high resonance degeneracy. To tackle this issue, we combine reverse labeling of amino acids, frequency-selective dipolar dephasing, and NMR difference spectroscopy. These methods have resulted in nearly complete resonance assignments of the transmembrane domain of human LR11 (SorLA) protein in E. coli membranes. To reduce background signals from E. coli lipids and proteins and improve spectral sensitivity, we effectively utilize amylose affinity chromatography to prepare membrane vesicles when MBP is included as a fusion partner in the expression construct.
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Registered trials
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