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Default Optimizing water hyperpolarization and dissolution for sensitivity-enhanced 2D biomolecular NMR

Optimizing water hyperpolarization and dissolution for sensitivity-enhanced 2D biomolecular NMR

Publication date: March 2016
Source:Journal of Magnetic Resonance, Volume 264

Author(s): Greg Olsen, Evgeny Markhasin, Or Szekely, Christian Bretschneider, Lucio Frydman

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 T 1 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 1H polarization enhancements over 11.7T thermal counterparts, long T 1 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 100500 over their optimized, thermally-polarized, counterparts.
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