Optimizing water hyperpolarization and dissolution for sensitivity-enhanced 2D biomolecular NMR
| Autor: | Lucio Frydman, Christian O. Bretschneider, Or Szekely, Evgeny Markhasin, Greg L. Olsen |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Nuclear and High Energy Physics
Proton Biophysics Analytical chemistry 010402 general chemistry 01 natural sciences Biochemistry chemistry.chemical_compound Electromagnetic Fields Amide Humans Hyperpolarization (physics) Amino Acids Dissolution Nuclear Magnetic Resonance Biomolecular Protein Unfolding chemistry.chemical_classification Spectrometer 010405 organic chemistry Biomolecule Proteins Reproducibility of Results Water Condensed Matter Physics Amides 0104 chemical sciences Solvent chemistry Solubility Chemical physics Protons Two-dimensional nuclear magnetic resonance spectroscopy Tomography Optical Coherence |
| Zdroj: | Journal of magnetic resonance (San Diego, Calif. : 1997). 264 |
| ISSN: | 1096-0856 |
| Popis: | A recent study explored the use of hyperpolarized water, to enhance the sensitivity of nuclei in biomolecules thanks to rapid proton exchanges with labile amide backbone and sidechain groups. Further optimizations of this approach have now allowed us to achieve proton polarizations approaching 25% in the water transferred into the NMR spectrometer, effective water T1 times approaching 40s, and a reduction in the dilution demanded for the cryogenic dissolution process. Further hardware developments have allowed us to perform these experiments, repeatedly and reliably, in 5mm NMR tubes. All these ingredients--particularly the ⩾ 3000× (1)H polarization enhancements over 11.7T thermal counterparts, long T1 times and a compatibility with high-resolution biomolecular NMR setups - augur well for hyperpolarized 2D NMR studies of peptides, unfolded proteins and intrinsically disordered systems undergoing fast exchanges of their protons with the solvent. This hypothesis is here explored by detailing the provisions that lead to these significant improvements over previous reports, and demonstrating 1D coherence transfer experiments and 2D biomolecular HMQC acquisitions delivering NMR spectral enhancements of 100-500× over their optimized, thermally-polarized, counterparts. |
| Databáze: | OpenAIRE |
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