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  • A 10,000-fold nuclear hyperpolarization of a membrane protein in the liquid phase via a solid-state mechanism.

A 10,000-fold nuclear hyperpolarization of a membrane protein in the liquid phase via a solid-state mechanism.

Journal of the American Chemical Society (2011-10-04)
Eugenio Daviso, Geertje Jacoba Janssen, A Alia, Gunnar Jeschke, Jörg Matysik, Marco Tessari
摘要

Several techniques rely on electron-nuclear interactions to boost the polarization of nuclear spins in the solid phase. Averaging out of anisotropic interactions as a result of molecular tumbling strongly reduces the applicability of such hyperpolarization approaches in liquids. Here we show for the first time that anisotropic electron-nuclear interactions in solution can survive sufficiently long to generate nuclear spin polarization by the solid-state photo-CIDNP mechanism. A 10,000-fold NMR signal increase in solution was observed for a giant biomolecular complex of a photosynthetic membrane protein with a tumbling correlation time in the submicrosecond regime, corresponding to a molecular weight close to 1 MDa.

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Sigma-Aldrich
十二烷基二甲基氧化胺 溶液, ~30% in H2O
Sigma-Aldrich
十二烷基二甲基氧化胺, BioXtra, ≥99.0% (NT)