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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0015-35BD-B Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-CBA9-3
Genre: Journal Article

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 Creators:
Fricke, P.1, Author           
Demers, J. P.1, Author           
Becker, S.2, Author           
Lange, A.1, Author           
Affiliations:
1Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: dynamic nuclear polarization; proteins; solid-state nmr; structure elucidation; type-three secretion system
 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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Language(s): eng - English
 Dates: 2013-11-26
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1002/cphc.201300994
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Title: ChemPhysChem
Source Genre: Journal
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Pages: - Volume / Issue: 15 (1) Sequence Number: - Start / End Page: 57 - 60 Identifier: ISSN: 1439-4235