ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2009
Labeling strategies for 13C-detected aligned-sample solid-state NMR of proteins.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed, 21 citations in OpenAlex.
- Cell-free synthesis of proteins with selectivelyMagnetic resonance (Gottingen, Germany) · 2023Article
- Evaluation of integrin αvβNature communications · 2019Article
- Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.The journal of physical chemistry. B · 2013Article
- Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012Article
- Structure determination of membrane proteins in five easy pieces.Methods (San Diego, Calif.) · 2011Review
- A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- (1)H-(13)C Hetero-nuclear dipole-dipole couplings of methyl groups in stationary and magic angle spinning solid-state NMR experiments of peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
(13)C-detected solid-state NMR experiments have substantially higher sensitivity than the corresponding (15)N-detected experiments on stationary, aligned samples of isotopically labeled proteins. Several methods for tailoring the isotopic labeling are described that result in spatially isolated (13)C sites so that dipole-dipole couplings among the (13)C are minimized, thus eliminating the need for homonuclear (13)C-(13)C decoupling in either indirect or direct dimensions of one- or multi-dimensional NMR experiments that employ (13)C detection. The optimal percentage for random fractional (13)C labeling is between 25% and 35%. Specifically labeled glycerol and glucose can be used at the carbon sources to tailor the isotopic labeling, and the choice depends on the resonances of interest for a particular study. For investigations of the protein backbone, growth of the bacteria on [2-(13)C]-glucose-containing media was found to be most effective.
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