title: Studies on the MxiH protein in T3SS needles using DNP-enhanced ssNMR spectroscopy.
abstract: 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.
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany).
authors.forename: Pascal
authors.initials: P
authors.lastname: Fricke
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Demers
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods
chemical_list: D001426:Bacterial Proteins; C413572:MxiH protein, Shigella
keywords: dynamic nuclear polarization; proteins; solid-state nmr; structure elucidation; type-three secretion system