ArticleJournal of biomolecular NMR2023
Strategies for acquisition of resonance assignment spectra of highly dynamic membrane proteins: a GPCR case study.
Article in Journal of biomolecular NMR, 2023. 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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Who cites it
2 citing papers in PubMed.
- Assessing the potential for Crude Oil degradation by Biosurfactant-producing Bacteria isolated from Marine Ecosystems in Nigeria.Access microbiology · 2026Article
- An in silico framework to visualize how cancer-associated mutations influence structural plasticity of the chemokine receptor CCR3.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
In protein nuclear magnetic resonance (NMR), chemical shift assignment provides a wealth of information. However, acquisition of high-quality solid-state NMR spectra depends on protein-specific dynamics. For membrane proteins, bilayer heterogeneity further complicates this observation. Since the efficiency of cross-polarization transfer is strongly entwined with protein dynamics, optimal temperatures for spectral sensitivity and resolution will depend not only on inherent protein dynamics, but temperature-dependent phase properties of the bilayer environment. We acquired 1-, 2-, and 3D homo- and heteronuclear experiments of the chemokine receptor CCR3 in a 7:3 phosphatidylcholine:cholesterol lipid environment. 1D direct polarization, cross polarization (CP), and T
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