ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2010
(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.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Dynamics in Flexible Pillar[The journal of physical chemistry. C, Nanomaterials and interfaces · 2021Article
- (14)N overtone NMR under MAS: signal enhancement using symmetry-based sequences and novel simulation strategies.Physical chemistry chemical physics : PCCP · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Experiments optimized for magic angle spinning and oriented sample solid-state NMR of proteins.The journal of physical chemistry. B · 2013Article
- Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- 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
- Proton evolved local field solid-state nuclear magnetic resonance using Hadamard encoding: theory and application to membrane proteins.The Journal of chemical physics · 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
- Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Journal of the American Chemical Society · 2010Article
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3 authors.
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Abstract
(13)C NMR of isotopically labeled methyl groups has the potential to combine spectroscopic simplicity with ease of labeling for protein NMR studies. However, in most high resolution separated local field experiments, such as polarization inversion spin exchange at the magic angle (PISEMA), that are used to measure (1)H-(13)C hetero-nuclear dipolar couplings, the four-spin system of the methyl group presents complications. In this study, the properties of the (1)H-(13)C hetero-nuclear dipolar interactions of (13)C-labeled methyl groups are revealed through solid-state NMR experiments on a range of samples, including single crystals, stationary powders, and magic angle spinning of powders, of (13)C(3) labeled alanine alone and incorporated into a protein. The spectral simplifications resulting from proton detected local field (PDLF) experiments are shown to enhance resolution and simplify the interpretation of results on single crystals, magnetically aligned samples, and powders. The complementarity of stationary sample and magic angle spinning (MAS) measurements of dipolar couplings is demonstrated by applying polarization inversion spin exchange at the magic angle and magic angle spinning (PISEMAMAS) to unoriented samples.
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