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Optimization of <sup>15</sup>N-<sup>13</sup>C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions.


ABSTRACT: Dynamic nuclear polarization (DNP) enhanced magic angle spinning (MAS) solid-state NMR carried out at 25 K enables rapid acquisition of multi-dimensional 13C-15N correlation spectra for protein structure studies and resonance assignment. Under commonly used DNP conditions, solvent deuteration reduces 1H-15N cross polarization (CP) efficiencies, necessitates more careful optimization, and requires longer high-power 15N radio-frequency pulses. The sensitivity of 2D heteronuclear correlation experiments is potentially impaired. Here we show that 2D 15N-13C experiments based on 13C-15N transferred echo double resonance (TEDOR) methods outperform 2D experiments based on CP transfers in a fully deu

SUBMITTER: Blake Wilson C 

PROVIDER: S-EPMC11573627 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature