In-cell NMR, solid-state NMR of bryostatin, and DNP-NMR of membrane proteins

In conventional (non-DNP) NMR experiments, we demonstrated that bryostatin adopts multiple conformations while bound to the C1b regulatory domain of PKC. Isotopic 19F, 2H, and 13C sites incorporated into bryostatin allowed us to measure very high-quality, long-range distances with rotational echo double resonance (REDOR) NMR. We previously employed MAS DNP-NMR to determine molecular structures within membranes including bacteriorhodopsin and the M2 influenza protein.