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A 10鈥?00-fold Nuclear Hyperpolarization of a Membrane Protein in the Liquid Phase via a Solid-State Mechanism
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文摘
Several techniques rely on electron鈥搉uclear 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鈥搉uclear interactions in solution can survive sufficiently long to generate nuclear spin polarization by the solid-state photo-CIDNP mechanism. A 10鈥?00-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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