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

Fricke, P.; Demers, J. P.; Becker, S.; Lange, A.

doi:10.1002/cphc.201300994

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

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Fricke, P.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Demers, J. P.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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Becker, S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lange, A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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1921083_Suppl_1.pdf
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Citation

Fricke, P., Demers, J. P., Becker, S., & Lange, A. (2013). Studies on the MxiH protein in T3SS needles using DNP-enhanced ssNMR spectroscopy. ChemPhysChem, 15(1), 57-60. doi:10.1002/cphc.201300994.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-35BD-B

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.