ArticleProtein science : a publication of the Protein Society2012
In situ 19F NMR studies of an E. coli membrane protein.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 31 citations in OpenAlex.
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025Review
- The Conformational Equilibria of a Human GPCR Compared between Lipid Vesicles and Aqueous Solutions by IntegrativeJournal of the American Chemical Society · 2025Article
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment.Biophysical journal · 2021Article
- De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Protein-protein interaction analysis in crude bacterial lysates using combinational method ofProtein & cell · 2017Article
- In-Cell Solid-State NMR: An Emerging Technique for the Study of Biological Membranes.Biophysical journal · 2015Review
- Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using (19)F nuclear magnetic resonance.Protein & cell · 2015Article
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
- Membrane proteins, magic-angle spinning, and in-cell NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this report, (19)F spin incorporation in a specific site of a specific membrane protein in E. coli was accomplished via trifluoromethyl-phenylalanine ((19) F-tfmF). Site-specific (19)F chemical shifts and longitudinal relaxation times of diacylglycerol kinase (DAGK), an E. coli membrane protein, were measured in its native membrane using in situ magic angle spinning (MAS) solid state nuclear magnetic resonance (NMR). Comparing with solution NMR data of the purified DAGK in detergent micelles, the in situ MAS-NMR data illustrated that (19)F chemical shift values of residues at different membrane protein locations were influenced by interactions between membrane proteins and their surrounding lipid or lipid mimic environments, while (19)F side chain longitudinal relaxation values were probably affected by different interactions of DAGK with planar lipid bilayer versus globular detergent micelles.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.