Temperature-Dependent Solid-State NMR Proton Chemical-Shift Values and Hydrogen Bonding
- Journal Article
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. Show more
Journal / seriesThe Journal of Physical Chemistry B
Pages / Article No.
PublisherAmerican Chemical Society
Organisational unit03496 - Meier, Beat H. / Meier, Beat H.
08829 - Ernst, Matthias (Tit.-Prof.)
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741863 - Faster magic-angle spinning leads to a resolution revolution in biological solid-state NMR (EC)
159707 - NMR studies in the Solid State (SNF)
188711 - NMR studies in the Solid State (SNF)
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