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Updated: Mar 19, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
The Chemical Shift Baseline for High-Pressure NMR Spectra of Proteins
Roland Frach1, Patrick Kibies1, Saraphina Böttcher1
1Physikalische Chemie III, Fakultät für Chemie und Chemische Biologie, TU Dortmund, Otto-Hahn-Strasse 4a, 44227, Dortmund, Germany.
Abstract:
High-pressure (HP) NMR spectroscopy is an important method for detecting rare functional states of proteins by analyzing the pressure response of chemical shifts. However, for the analysis of the shifts it is mandatory to understand the origin of the observed pressure dependence. Here we present experimental HP NMR data on the (15) N-enriched peptide bond model, N-methylacetamide (NMA), in water, combined with quantum-chemical computations of the magnetic parameters using a pressure-sensitive solvation model. Theoretical analysis of NMA and the experimentally used internal reference standard 4,4-dimethyl-4-silapentane-1-sulfonic (DSS) reveal that a substantial part of observed shifts can be attributed to purely solvent-induced electronic polarization of the backbone. DSS is only marginally responsive to pressure changes and is therefore a reliable sensor for variations in the local magnetic field caused by pressure-induced changes of the magnetic susceptibility of the solvent.
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