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  • 2014Journal Article
    [["dc.bibliographiccitation.artnumber","e112374"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Yao, Xuejun"],["dc.contributor.author","Duerr, Ulrich H. N."],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Laukat, Yvonne"],["dc.contributor.author","Narayanan, Rhagavendran L."],["dc.contributor.author","Brueckner, Ann-Kathrin"],["dc.contributor.author","Meisinger, Chris"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:32:43Z"],["dc.date.available","2018-11-07T09:32:43Z"],["dc.date.issued","2014"],["dc.description.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."],["dc.identifier.doi","10.1371/journal.pone.0112374"],["dc.identifier.isi","000344402600137"],["dc.identifier.pmid","25375235"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11135"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31809"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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