ArticleJournal of the American Chemical Society2013
Multidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 71 citations in OpenAlex.
- Windowed Symmetry Pulses for Enhanced Heteronuclear Dipolar Recoupling in Solid-State MAS NMR.Precision chemistry · 2026Article
- Analyzing atomic scale structural details and nuclear spin dynamics of four macrolide antibiotics: erythromycin, clarithromycin, azithromycin, and roxithromycin.RSC advances · 2024Article
- Simultaneous recoupling of chemical shift tensors of two nuclei by R-symmetry sequences.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- Review
- Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Methods (San Diego, Calif.) · 2018Review
- Backbone amideSolid state nuclear magnetic resonance · 2018Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz.Solid state nuclear magnetic resonance · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD.Journal of the American Chemical Society · 2016Article
- Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences.Physical chemistry chemical physics : PCCP · 2016Article
- RF inhomogeneity and how it controls CPMAS.Solid state nuclear magnetic resonance · 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
- Internal dynamics of dynactin CAP-Gly is regulated by microtubules and plus end tracking protein EB1.The Journal of biological chemistry · 2015Article
- Composite-180° pulse-based symmetry sequences to recouple proton chemical shift anisotropy tensors under ultrafast MAS solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.Journal of biomolecular NMR · 2014Article
- Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.Biochemistry · 2014Article
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5 authors at 2 institutions in 1 country.
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Abstract
The proton chemical shift (CS) tensor is a sensitive probe of structure and hydrogen bonding. Highly accurate quantum-chemical protocols exist for computation of (1)H magnetic shieldings in the various contexts, making proton chemical shifts potentially a powerful predictor of structural and electronic properties. However, (1)H CS tensors are not yet widely used in protein structure calculation due to scarcity of experimental data. While isotropic proton shifts can be readily measured in proteins even in the solid state, determination of the (1)H chemical shift anisotropy (CSA) tensors remains challenging, particularly in molecules containing multiple proton sites. We present a method for site-resolved measurement of amide proton CSAs in fully protonated solids under magic angle spinning. The approach consists of three concomitant 3D experiments yielding spectra determined by either mainly (1)H CSA, mainly (1)H–(15)N dipolar, or combined (1)H CSA and (1)H–(15)N dipolar interactions. The anisotropic interactions are recoupled using RN-sequences of appropriate symmetry, such as R12(1)(4), and (15)N/(13)C isotropic CS dimensions are introduced via a short selective (1)H–(15)N cross-polarization step. Accurate (1)H chemical shift tensor parameters are extracted by simultaneous fit of the lineshapes recorded in the three spectra. An application of this method is presented for an 89-residue protein, U-(13)C,(15)N-CAP-Gly domain of dynactin. The CSA parameters determined from the triple fits correlate with the hydrogen-bonding distances, and the trends are in excellent agreement with the prior solution NMR results. This approach is generally suited for recording proton CSA parameters in various biological and organic systems, including protein assemblies and nucleic acids.
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