ArticleThe journal of physical chemistry. B2021
Temperature-Dependent Solid-State NMR Proton Chemical-Shift Values and Hydrogen Bonding.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Ultrahigh-resolution solid-state NMR for high-molecular weight proteins on GHz-class spectrometers.Science advances · 2025Article
- High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz.Chemical science · 2023Article
- Review
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Correction of field instabilities in biomolecular solid-state NMR by simultaneous acquisition of a frequency reference.Magnetic resonance (Gottingen, Germany) · 2022Article
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Residual dipolar line width in magic-angle spinning proton solid-state NMR.Magnetic resonance (Gottingen, Germany) · 2021Article
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Authors and funding
8 authors.
Funding
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Abstract
Temperature-dependent NMR experiments are often complicated by rather long magnetic-field equilibration times, for example, occurring upon a change of sample temperature. We demonstrate that the fast temporal stabilization of a magnetic field can be achieved by actively stabilizing the temperature of the magnet bore, which allows quantification of the weak temperature dependence of a proton chemical shift, which can be diagnostic for the presence of hydrogen bonds. Hydrogen bonding plays a central role in molecular recognition events from both fields, chemistry and biology. Their direct detection by standard structure-determination techniques, such as X-ray crystallography or cryo-electron microscopy, remains challenging due to the difficulties of approaching the required resolution, on the order of 1 Å. We, herein, explore a spectroscopic approach using solid-state NMR to identify protons engaged in hydrogen bonds and explore the measurement of proton chemical-shift temperature coefficients. Using the examples of a phosphorylated amino acid and the protein ubiquitin, we show that fast magic-angle spinning (MAS) experiments at 100 kHz yield sufficient resolution in proton-detected spectra to quantify the rather small chemical-shift changes upon temperature variations.
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