Frach, Roland and Kibies, Patrick and Boettcher, Saraphina and Pongratz, Tim and Strohfeldt, Steven and Kurrmann, Simon and Koehler, Joerg and Hofmann, Martin and Kremer, Werner and Kalbitzer, Hans Robert and Reiser, Oliver and Horinek, Dominik and Kast, Stefan M. (2016) The Chemical Shift Baseline for High-Pressure NMR Spectra of Proteins. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 55 (30). pp. 8757-8760. ISSN 1433-7851, 1521-3773
Full text not available from this repository. (Request a copy)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 N-15-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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