Bauch, Susanne

[["dc.bibliographiccitation.firstpage","2059"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","2068"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Vainio, Ulla"],["dc.contributor.author","Wedig, Tatjana"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","The assembly kinetics of intermediate filament (IF) proteins from tetrameric complexes to single filaments and networks depends on the protein concentration, temperature and the ionic composition of their environment. We systematically investigate how changes in the concentration of monovalent potassium and divalent magnesium ions affect the internal organization of the resulting filaments. Small angle X-ray scattering (SAXS) is very sensitive to changes in the filament cross-section such as diameter or compactness. Our measurements reveal that filaments formed in the presence of magnesium chloride differ distinctly from filaments formed in the presence of potassium chloride. The principle multi-step assembly mechanism from tetramers via unit-length filaments (ULF) to elongated filaments is not changed by the valency of ions. However, the observed differences indicate that the magnesium ions free the head domains of tetramers from unproductive interactions to allow assembly but at the same time mediate strong inter-tetrameric interactions that impede longitudinal annealing of unit-length filaments considerably, thus slowing down filament growth."],["dc.identifier.doi","10.1039/c3sm52532e"],["dc.identifier.gro","3142216"],["dc.identifier.isi","000332463300021"],["dc.identifier.pmid","24800271"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5821"],["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","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.contributor.author","Lorenz, Charlotta"],["dc.contributor.author","Forsting, Johanna"],["dc.contributor.author","Schepers, Anna V."],["dc.contributor.author","Kraxner, Julia"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Klumpp, Stefan"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2020-03-03T08:23:45Z"],["dc.date.available","2020-03-03T08:23:45Z"],["dc.date.issued","2019"],["dc.description.abstract","The cytoskeleton is a composite network of three types of protein filaments, among which in-termediate filaments (IFs) are the most extensible ones. Two very important IFs are keratin and vimentin, which have similar molecular architectures, but different mechanical behaviors. Here we compare the mechanical response of single keratin and vimentin filaments using optical tweezers. We show that the mechanics of vimentin strongly depends on the ionic strength of the buffer and that its force-strain curve suggests a high degree of cooperativity between subunits. Indeed, a computational model indicates that in contrast to keratin, vimentin is characterized by strong lateral subunit coupling of its charged monomers during unfolding of α-helices. We conclude that cells can tune their mechanics by differential use of keratin versus vimentin."],["dc.identifier.doi","10.1101/676197"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16475"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63071"],["dc.language.iso","en"],["dc.title","Lateral Subunit Coupling Determines Intermediate Filament Mechanics"],["dc.type","preprint"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]