NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins

2014 | journal article. A publication with affiliation to the University of Göttingen.

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​NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins​
Yao, X.; Duerr, U. H. N.; Gattin, Z.; Laukat, Y.; Narayanan, R. L.; Brueckner, A.-K. & Meisinger, C. et al.​ (2014) 
PLoS ONE9(11) art. e112374​.​ DOI: https://doi.org/10.1371/journal.pone.0112374 

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Authors
Yao, Xuejun; Duerr, Ulrich H. N.; Gattin, Zrinka; Laukat, Yvonne; Narayanan, Rhagavendran L.; Brueckner, Ann-Kathrin; Meisinger, Chris; Lange, Adam; Becker, Stefan; Zweckstetter, Markus
Abstract
Membrane proteins play key roles in biology. Determination of their structure in a membrane environment, however, is highly challenging. To address this challenge, we developed an approach that couples hydrogen/deuterium exchange of membrane proteins to rapid unfolding and detection by solution-state NMR spectroscopy. We show that the method allows analysis of the solvent protection of single residues in liposome-embedded proteins such as the 349-residue Tom40, the major protein translocation pore in the outer mitochondrial membrane, which has resisted structural analysis for many years.
Issue Date
2014
Status
published
Publisher
Public Library Science
Journal
PLoS ONE 
ISSN
1932-6203

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