DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins.

ABSTRACT: Dynamic nuclear polarization (DNP) enables dramatic sensitivity enhancements of solid-state nuclear magnetic resonance (NMR) spectra for biological systems to be realized via polarization transfer from unpaired electrons of a polarizing agent, typically a nitroxide biradical, to nuclear spins of the system of interest. Here, we systematically investigate the prospect of recording DNP enhanced solid-state NMR spectra of hydrated lattice-like protein assemblies within sample formulations that are free of the commonly employed glycerol-based glassy solvent matrix containing exogenous polarizing agent molecules and instead consist of isotope-enriched protein of interest co-assembled with its dinitroxide-tagged structural analog incorporated as a dopant at low concentration. As a model system w

SUBMITTER: O'Neil CM 

PROVIDER: S-EPMC12810707 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature