Wednesday, December 21, 2011

A 10‚000-fold Nuclear Hyperpolarization of a Membrane Protein in the Liquid Phase via a Solid-State Mechanism

Daviso, E., et al., A 10‚000-fold Nuclear Hyperpolarization of a Membrane Protein in the Liquid Phase via a Solid-State Mechanism. J. Am. Chem. Soc., 2011. 133(42): p. 16754-16757.


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.