ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2014
3D ¹⁵N/¹⁵N/¹H chemical shift correlation experiment utilizing an RFDR-based ¹H/¹H mixing period at 100 kHz MAS.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 63 citations in OpenAlex.
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- Homonuclear Chemical Shift Correlation in Solids Under MAS by Fast Cross-Relaxation Driven Spin Diffusion.bioRxiv : the preprint server for biology · 2025Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
- Optimisation ofPhysical chemistry chemical physics : PCCP · 2022Article
- Modest Offset Difference Internuclear Selective Transfer via Homonuclear Dipolar Coupling.The journal of physical chemistry letters · 2022Article
- Efficient solvent suppression with adiabatic inversion forJournal of biomolecular NMR · 2021Article
- Residual dipolar line width in magic-angle spinning proton solid-state NMR.Magnetic resonance (Gottingen, Germany) · 2021Article
- Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021Article
- Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.The journal of physical chemistry. B · 2020Article
- Homonuclear Decoupling inAngewandte Chemie (International ed. in English) · 2020Article
- Nucleotide Binding Modes in a Motor Protein Revealed byChembiochem : a European journal of chemical biology · 2020Article
- Fast electron paramagnetic resonance magic angle spinning simulations using analytical powder averaging techniques.The Journal of chemical physics · 2019Article
- Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy.Accounts of chemical research · 2017Review
- Enhancing NMR Sensitivity of Natural-Abundance Low-γ Nuclei by Ultrafast Magic-Angle-Spinning Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 1020MHz single-channel proton fast magic angle spinning solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Proton-detected 3D (1)H/(13)C/(1)H correlation experiment for structural analysis in rigid solids under ultrafast-MAS above 60 kHz.The Journal of chemical physics · 2015Article
- Proton chemical shift tensors determined by 3D ultrafast MAS double-quantum NMR spectroscopy.The Journal of chemical physics · 2015Article
- Selective excitation enables assignment of proton resonances and (1)H-(1)H distance measurement in ultrafast magic angle spinning solid state NMR spectroscopy.The Journal of chemical physics · 2015Article
- Proton-Detected Solid-State NMR Spectroscopy of Bone with Ultrafast Magic Angle Spinning.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Homonuclear correlation NMR experiments are commonly used in the high-resolution structural studies of proteins. While (13)C/(13)C chemical shift correlation experiments utilizing dipolar recoupling techniques are fully utilized under MAS, correlation of the chemical shifts of (15)N nuclei in proteins has been a challenge. Previous studies have shown that the negligible (15)N-(15)N dipolar coupling in peptides or proteins necessitates the use of a very long mixing time (typically several seconds) for effective spin diffusion to occur and considerably slows down a (15)N/(15)N correlation experiment. In this study, we show that the use of mixing proton magnetization, instead of (15)N, via the recoupled (1)H-(1)H dipolar couplings enable faster (15)N/(15)N correlation. In addition, the use of proton-detection under ultrafast MAS overcomes the sensitivity loss due to multiple magnetization transfer (between (1)H and (15)N nuclei) steps. In fact, less than 300 nL (∼1.1 micromole quantity) sample is sufficient to acquire the 3D spectrum within 5 h. Our results also demonstrate that a 3D (15)N/(15)N/(1)H experiment can render higher resolution spectra that will be useful in the structural studies of proteins at ultrafast MAS frequencies. 3D (15)N/(15)N/(1)H and 2D radio frequency-driven dipolar recoupling (RFDR)-based (1)H/(1)H experimental results obtained from a powder sample of N-acetyla-L-(15)N-valyl-L-(15)N-leucine at 70 and 100kHz MAS frequencies are presented.
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