ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2012
Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- Conformation-selective detection of residues in solid proteins under magic-angle-spinning.Journal of biomolecular NMR · 2026Article
- Great Offset Difference Internuclear Selective Transfer.The journal of physical chemistry letters · 2023Article
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Multi-receiver solid-state NMR using polarization optimized experiments (POE) at ultrafast magic angle spinning.Journal of biomolecular NMR · 2020Article
- Structural characterization of the D290V mutation site in hnRNPA2 low-complexity-domain polymers.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance.Cold Spring Harbor perspectives in medicine · 2016Review
- Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences.Physical chemistry chemical physics : PCCP · 2016Article
- Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- MAS NMR of HIV-1 protein assemblies.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Phase cycling schemes for finite-pulse-RFDR MAS solid state NMR experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- 3D ¹⁵N/¹⁵N/¹H chemical shift correlation experiment utilizing an RFDR-based ¹H/¹H mixing period at 100 kHz MAS.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Site-specific structural variations accompanying tubular assembly of the HIV-1 capsid protein.Journal of molecular biology · 2014Article
- Article
- Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures.Protein science : a publication of the Protein Society · 2012Article
- Fiber diffraction data indicate a hollow core for the Alzheimer's aβ 3-fold symmetric fibril.Journal of molecular biology · 2012Article
- Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance.The Journal of chemical physics · 2012Article
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5 authors.
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Abstract
Recent structural studies of uniformly (15)N, (13)C-labeled proteins by solid state nuclear magnetic resonance (NMR) rely principally on two sources of structural restraints: (i) restraints on backbone conformation from isotropic (15)N and (13)C chemical shifts, based on empirical correlations between chemical shifts and backbone torsion angles; (ii) restraints on inter-residue proximities from qualitative measurements of internuclear dipole-dipole couplings, detected as the presence or absence of inter-residue crosspeaks in multidimensional spectra. We show that site-specific dipole-dipole couplings among (15)N-labeled backbone amide sites and among (13)C-labeled backbone carbonyl sites can be measured quantitatively in uniformly-labeled proteins, using dipolar recoupling techniques that we call (15)N-BARE and (13)C-BARE (BAckbone REcoupling), and that the resulting data represent a new source of restraints on backbone conformation. (15)N-BARE and (13)C-BARE data can be incorporated into structural modeling calculations as potential energy surfaces, which are derived from comparisons between experimental (15)N and (13)C signal decay curves, extracted from crosspeak intensities in series of two-dimensional spectra, with numerical simulations of the (15)N-BARE and (13)C-BARE measurements. We demonstrate this approach through experiments on microcrystalline, uniformly (15)N, (13)C-labeled protein GB1. Results for GB1 show that (15)N-BARE and (13)C-BARE restraints are complementary to restraints from chemical shifts and inter-residue crosspeaks, improving both the precision and the accuracy of calculated structures.
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