Publication details
High-Resolution NMR of Folded Proteins in Hyperpolarized Physiological Solvents
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Article in Periodical |
| Magazine / Source | Chemistry - A European Journal |
| MU Faculty or unit | |
| Citation | |
| web | https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201802885 |
| Doi | https://doi.org/10.1002/chem.201802885 |
| Keywords | dissolution DNP; hyperpolarized water; cross-relaxation effect; protein NMR spectroscopy; proton exchange |
| Description | 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. |