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The Chemical Shift Baseline for High‐Pressure NMR Spectra of Proteins
Author(s) -
Frach Roland,
Kibies Patrick,
Böttcher Saraphina,
Pongratz Tim,
Strohfeldt Steven,
Kurrmann Simon,
Koehler Joerg,
Hofmann Martin,
Kremer Werner,
Kalbitzer Hans Robert,
Reiser Oliver,
Horinek Dominik,
Kast Stefan M.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201602054
Subject(s) - chemical shift , chemistry , solvation , nuclear magnetic resonance spectroscopy , polarization (electrochemistry) , quantum chemical , solvent , nmr spectra database , spectral line , spectroscopy , computational chemistry , chemical physics , nuclear magnetic resonance , molecule , organic chemistry , physics , quantum mechanics , astronomy
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.