- 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
PMID21962225
RÉSUMÉ
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.