KADEŘÁVEK, Pavel, F. FERRAGE, G. BODENHAUSEN and D. KURZBACH. High-Resolution NMR of Folded Proteins in Hyperpolarized Physiological Solvents. Chemistry - A European Journal. WEINHEIM: Wiley, 2018, vol. 24, No 51, p. 13418-13423. ISSN 0947-6539. Available from: https://dx.doi.org/10.1002/chem.201802885.
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Basic information
Original name High-Resolution NMR of Folded Proteins in Hyperpolarized Physiological Solvents
Authors KADEŘÁVEK, Pavel (203 Czech Republic, guarantor, belonging to the institution), F. FERRAGE (250 France), G. BODENHAUSEN (250 France) and D. KURZBACH (250 France).
Edition Chemistry - A European Journal, WEINHEIM, Wiley, 2018, 0947-6539.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10402 Inorganic and nuclear chemistry
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 5.160
RIV identification code RIV/00216224:14740/18:00104510
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1002/chem.201802885
UT WoS 000444413700006
Keywords in English dissolution DNP; hyperpolarized water; cross-relaxation effect; protein NMR spectroscopy; proton exchange
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 13/3/2019 11:20.
Abstract
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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