ArticleMagnetic resonance in chemistry : MRC2007
Tailoring 13C labeling for triple-resonance solid-state NMR experiments on aligned samples of proteins.
Article in Magnetic resonance in chemistry : MRC, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2013Review
- Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Structure determination of membrane proteins in five easy pieces.Methods (San Diego, Calif.) · 2011Review
- 1H assisted 13C/15N heteronuclear correlation spectroscopy in oriented sample solid-state NMR of single crystal and magnetically aligned samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- 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
- 1H-13C separated local field spectroscopy of uniformly 13C labeled peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- (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
- Labeling strategies for 13C-detected aligned-sample solid-state NMR of proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- A strip-shield improves the efficiency of a solenoid coil in probes for high-field solid-state NMR of lossy biological samples.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
In order to develop triple-resonance solid-state NMR spectroscopy of membrane proteins, we have implemented several different (13)C labeling schemes with the purpose of overcoming the interfering effects of (13)C-(13)C dipole-dipole couplings in stationary samples. The membrane-bound form of the major coat protein of the filamentous bacteriophage Pf1 was used as an example of a well-characterized helical membrane protein. Aligned protein samples randomly enriched to 35% (13)C in all sites and metabolically labeled from bacterial growth on media containing [2-(13)C]-glycerol or [1,3-(13)C]-glycerol enables direct (13)C detection in solid-state NMR experiments without the need for homonuclear (13)C-(13)C dipole-dipole decoupling. The (13)C-detected NMR spectra of Pf1 coat protein show a substantial increase in sensitivity compared to the equivalent (15)N-detected spectra. The isotopic labeling pattern was analyzed for [2-(13)C]-glycerol and [1,3-(13)C]-glycerol as metabolic precursors by solution-state NMR of micelle samples. Polarization inversion spin exchange at the magic angle (PISEMA) and other solid-state NMR experiments work well on 35% random fractionally and metabolically tailored (13)C-labeled samples, in contrast to their failure with conventional 100% uniformly (13)C-labeled samples.
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