Informace o publikaci

High-Resolution NMR of Folded Proteins in Hyperpolarized Physiological Solvents

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KADEŘÁVEK Pavel FERRAGE F. BODENHAUSEN G. KURZBACH D.

Druh Článek v odborném periodiku
Časopis / Zdroj Chemistry - A European Journal
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201802885
Doi http://dx.doi.org/10.1002/chem.201802885
Klíčová slova dissolution DNP; hyperpolarized water; cross-relaxation effect; protein NMR spectroscopy; proton exchange
Popis 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.