ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2007
Triple resonance experiments for aligned sample solid-state NMR of (13)C and (15)N labeled proteins.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 28 citations in OpenAlex.
- Validation of protein backbone structures calculated from NMR angular restraints using Rosetta.Journal of biomolecular NMR · 2019Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- 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
- 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 Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers.Journal of biomolecular NMR · 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
- Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.The journal of physical chemistry. B · 2010Article
- 1H-13C separated local field spectroscopy of uniformly 13C labeled peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- Sensitivity enhanced heteronuclear correlation spectroscopy in multidimensional solid-state NMR of oriented systems via chemical shift coherences.Journal of the American Chemical Society · 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
- Shiftless nuclear magnetic resonance spectroscopy.The Journal of chemical physics · 2008Article
- Tailoring 13C labeling for triple-resonance solid-state NMR experiments on aligned samples of proteins.Magnetic resonance in chemistry : MRC · 2007Article
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5 authors at 1 institution in 1 country.
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Abstract
Initial steps in the development of a suite of triple-resonance (1)H/(13)C/(15)N solid-state NMR experiments applicable to aligned samples of (13)C and (15)N labeled proteins are described. The experiments take advantage of the opportunities for (13)C detection without the need for homonuclear (13)C/(13)C decoupling presented by samples with two different patterns of isotopic labeling. In one type of sample, the proteins are approximately 20% randomly labeled with (13)C in all backbone and side chain carbon sites and approximately 100% uniformly (15)N labeled in all nitrogen sites; in the second type of sample, the peptides and proteins are (13)C labeled at only the alpha-carbon and (15)N labeled at the amide nitrogen of a few residues. The requirement for homonuclear (13)C/(13)C decoupling while detecting (13)C signals is avoided in the first case because of the low probability of any two (13)C nuclei being bonded to each other; in the second case, the labeled (13)C(alpha) sites are separated by at least three bonds in the polypeptide chain. The experiments enable the measurement of the (13)C chemical shift and (1)H-(13)C and (15)N-(13)C heteronuclear dipolar coupling frequencies associated with the (13)C(alpha) and (13)C' backbone sites, which provide orientation constraints complementary to those derived from the (15)N labeled amide backbone sites. (13)C/(13)C spin-exchange experiments identify proximate carbon sites. The ability to measure (13)C-(15)N dipolar coupling frequencies and correlate (13)C and (15)N resonances provides a mechanism for making backbone resonance assignments. Three-dimensional combinations of these experiments ensure that the resolution, assignment, and measurement of orientationally dependent frequencies can be extended to larger proteins. Moreover, measurements of the (13)C chemical shift and (1)H-(13)C heteronuclear dipolar coupling frequencies for nearly all side chain sites enable the complete three-dimensional structures of proteins to be determined with this approach.
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