Laukat, Yvonne

[["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"]]

[["dc.bibliographiccitation.firstpage","311"],["dc.bibliographiccitation.issue","3-4"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","320"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Laukat, Yvonne"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Maier, Elke"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:44:27Z"],["dc.date.available","2017-09-07T11:44:27Z"],["dc.date.issued","2015"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles."],["dc.identifier.doi","10.1007/s10858-014-9876-5"],["dc.identifier.gro","3141930"],["dc.identifier.isi","000352711900012"],["dc.identifier.pmid","25399320"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2657"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]