ausblenden:
Schlagwörter:
dynamic nuclear polarization; proteins; solid-state nmr; structure elucidation; type-three secretion system
Zusammenfassung:
Bacterial T3SS needles formed by the protein MxiH are studied using DNP-enhanced ssNMR spectroscopy at 14.1 T (600 MHz). This technique provides spectra of good resolution, allowing us to draw conclusions about the protein dynamics. With the obtained signal enhancement, samples of limited quantity now get within reach of ssNMR studies.