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High‐Resolution NMR of Folded Proteins in Hyperpolarized Physiological Solvents
Author(s) -
Kadeřávek Pavel,
Ferrage Fabien,
Bodenhausen Geoffrey,
Kurzbach Dennis
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201802885
Subject(s) - chemistry , hyperpolarization (physics) , nuclear magnetic resonance spectroscopy , solvent , nuclear magnetic resonance , two dimensional nuclear magnetic resonance spectroscopy , molecule , nmr spectra database , dissolution , relaxation (psychology) , analytical chemistry (journal) , spectral line , stereochemistry , chromatography , organic chemistry , psychology , social psychology , physics , astronomy
Hyperpolarized 2D exchange spectroscopy (HYPEX) to obtain high‐resolution nuclear magnetic resonance (NMR) spectra of folded proteins under near‐physiological conditions is reported. The technique is based on hyperpolarized water, which is prepared by dissolution dynamic nuclear polarization and mixed in situ in an NMR spectrometer with a protein in a physiological saline buffer at body temperature. Rapid exchange of labile protons with the hyperpolarized solvent, combined with cross‐relaxation effects (NOEs), leads to boosted signal intensities for many amide 1 H– 15 N correlations in the protein ubiquitin. As the introduction of hyperpolarization to the target protein is mediated via the solvent, the method is applicable to a broad spectrum of target molecules.