ArticleJournal of the American Chemical Society2010
Use of a copper-chelated lipid speeds up NMR measurements from membrane proteins.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 71 citations in OpenAlex.
- Lipid-nanodiscs formed by paramagnetic metal chelated polymer for fast NMR data acquisition.Biochimica et biophysica acta. Biomembranes · 2020Article
- Metal-Chelated Polymer Nanodiscs for NMR Studies.Angewandte Chemie (International ed. in English) · 2019Article
- Improving the quality of oriented membrane protein spectra using heat-compensated separated local field experiments.Journal of biomolecular NMR · 2019Article
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- Peptide bond conformation in peptides and proteins probed by dipolar coupling-chemical shift tensor correlation solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- 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
- New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Archives of biochemistry and biophysics · 2017Review
- GdJournal of biomolecular NMR · 2017Article
- Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-bScientific reports · 2017Article
- Sensitivity enhancement for membrane proteins reconstituted in parallel and perpendicular oriented bicelles obtained by using repetitive cross-polarization and membrane-incorporated free radicals.Journal of biomolecular NMR · 2017Article
- Evolution of CPMAS under fast magic-angle-spinning at 100 kHz and beyond.Solid state nuclear magnetic resonance · 2015Article
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization.Journal of biomolecular NMR · 2015Article
- Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.Biochimica et biophysica acta · 2015Article
- Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.Journal of biomolecular NMR · 2015Article
- Acceleration of natural-abundance solid-state MAS NMR measurements on bone by paramagnetic relaxation from gadolinium-DTPA.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd³⁺-complexes for solid-state NMR spectroscopy.Journal of biomolecular NMR · 2014Article
- High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning.Journal of biomolecular NMR · 2014Article
- Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning.Accounts of chemical research · 2013Article
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5 authors at 2 institutions in 2 countries.
Funding
Abstract
Recent studies have demonstrated the abilities of solid-state NMR techniques to solve atomic-level-resolution structures and dynamics of membrane-associated proteins and peptides. However, high-throughput applications of solid-state NMR spectroscopy are hampered by long acquisition times due to the low sensitivity of the technique. In this study, we demonstrate the use of a paramagnetic copper-chelated lipid to enhance the spin-lattice relaxation and thereby speed up solid-state NMR measurements. Fluid lamellar-phase bicelles composed of a lipid, detergent, and the copper-chelated lipid and containing a uniformly (15)N-labeled antimicrobial peptide, subtilosin A, were used at room temperature. The use of a chelating lipid reduces the concentration of free copper and limits RF-induced heating, a major problem for fluid samples. Our results demonstrate a 6.2-fold speed increase and a 2.7-fold improvement in signal-to-noise ratio for solid-state NMR experiments under magic-angle spinning and static conditions, respectively. Furthermore, solid-state NMR measurements are shown to be feasible even for nanomole concentrations of a membrane-associated peptide.
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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.