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      Studies on the MxiH protein in T3SS needles using DNP-enhanced ssNMR spectroscopy.

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          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.

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          Author and article information

          Journal
          Chemphyschem
          Chemphyschem : a European journal of chemical physics and physical chemistry
          Wiley-Blackwell
          1439-7641
          1439-4235
          Jan 13 2014
          : 15
          : 1
          Affiliations
          [1 ] Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany).
          Article
          10.1002/cphc.201300994
          24282046
          99d50e99-8a1b-4d7d-bf8d-6415d315b8d3
          History

          dynamic nuclear polarization,proteins,solid-state nmr,structure elucidation,type-three secretion system

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