Temperature-Dependent Solid-State NMR Proton Chemical-Shift Values and Hydrogen Bonding
Year: 2021
Type: article
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.
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $3,683
Funders: National Science Foundation, Deutsche Forschungsgemeinschaft, Agence Nationale de la Recherche, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, Eidgenössische Technische Hochschule Zürich, Agence Nationale de Recherches sur le Sida et les Hépatites Virales, H2020 European Research Council
Awards: G2222446239, G3010527862, G40186188, NMR studies in the Solid State, Dynamiques eco-évolutives des maladies infectieuses, Faster magic-angle spinning leads to a resolution revolution in biological solid-state NMR, G5599649393, G628552264, ProteinNukleinsäureErkennung untersucht durch FestkörperKernresonanzspektroskopie bei schnellen Rotationen um den magischen Winkel, G7656556208, Dissecting the molecular mechanism of an antibiotic efflux pump, NMR studies in the Solid State
OpenAlex ID: W3136310388