期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 24, 期 51, 页码 13418-13423出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201802885
关键词
dissolution DNP; hyperpolarized water; cross-relaxation effect; protein NMR spectroscopy; proton exchange
资金
- French CNRS
- ERC [339754, 279519]
- Equipex Paris-en-Resonance [ANR-10-EQPX-09]
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 H-1-N-15 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.
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