Bauch, Susanne

[["dc.bibliographiccitation.firstpage","1999"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","2008"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Vainio, Ulla"],["dc.contributor.author","Wedig, Tatjana"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2019-07-09T11:50:32Z"],["dc.date.available","2019-07-09T11:50:32Z"],["dc.date.issued","2019"],["dc.description.abstract","Vimentin intermediate filaments constitute a distinct filament system in mesenchymal cells that is instrumental for cellular mechanics and migration. In vitro, the rod-like monomers assemble in a multi-step, salt-dependent manner into micrometer long biopolymers. To disclose the underlying mechanisms further, we employed small angle X-ray scattering on two recombinant vimentin variants, whose assembly departs at strategic points from the normal assembly route: (i) vimentin with a tyrosine to leucine change at position 117; (ii) vimentin missing the non-α-helical carboxyl-terminal domain. Y117L vimentin assembles into unit-length filaments (ULFs) only, whereas ΔT vimentin assembles into filaments containing a higher number of tetramers per cross section than normal vimentin filaments. We show that the shape and inner structure of these mutant filaments is significantly altered. ULFs assembled from Y117L vimentin contain more, less tightly bundled vimentin tetramers, and ΔT vimentin filaments preserve the number density despite the higher number of tetramers per filament cross-section."],["dc.identifier.doi","10.1039/c8sm02281j"],["dc.identifier.pmid","30719518"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15958"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59791"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1744-6848"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0/"],["dc.subject.ddc","530"],["dc.subject.gro","cellular biophysics"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Intermediate Filaments"],["dc.subject.mesh","Mutation"],["dc.subject.mesh","Protein Subunits"],["dc.subject.mesh","Scattering, Small Angle"],["dc.subject.mesh","Vimentin"],["dc.subject.mesh","X-Ray Diffraction"],["dc.title","Mutation-induced alterations of intra-filament subunit organization in vimentin filaments revealed by SAXS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","708"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","716"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Nolting, Jens-Friedrich"],["dc.contributor.author","Dammann, Christian"],["dc.contributor.author","Noeding, Bernd"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Pfohl, Thomas"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:45:07Z"],["dc.date.available","2017-09-07T11:45:07Z"],["dc.date.issued","2011"],["dc.description.abstract","The assembly of intermediate filaments (IFs) is a complex process that can be recapitulated through a series of distinct steps in vitro. The combination of microfluidics and small angle X-ray scattering (SAXS) provides a powerful tool to investigate the kinetics of this process on the relevant timescales. Microfluidic mixers based on the principle of hydrodynamic focusing allow for precise control of the mixing of proteins and smaller reagents like ions. Here, we present a multi-layer device that prevents proteins from adsorbing to the channel walls by engulfing the protein jet with a fluid layer of buffer. To ensure compatibility with SAXS, the device is fabricated from UV-curable adhesive (NOA 81). To demonstrate the successful prevention of contact between the protein jet and the channel walls we measure the distribution of a fluorescent dye in the device by confocal microscopy at various flow speeds and compare the results to finite element method (FEM) simulations. The prevention of contact enables the investigation of the assembly of IFs in flow by gradually increasing the salt concentration in the protein jet. The diffusion of salt into the jet can be determined by FEM simulations. SAXS data are collected at different positions in the jet, corresponding to different salt concentrations, and they reveal distinct differences between the earliest assembly states. We find that the mean square radius of gyration perpendicular to the filament axis increases from 13 nm(2) to 58 nm(2) upon assembly. Thereby we provide dynamic structural data of a complex assembly process that was amenable up to now only by microscopic techniques."],["dc.identifier.doi","10.1039/c0lc00319k"],["dc.identifier.gro","3142804"],["dc.identifier.isi","000286765700019"],["dc.identifier.pmid","21212871"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10269"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/249"],["dc.language.iso","en"],["dc.notes","This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively."],["dc.notes.intern","WoS Import 2017-03-10 / Funder: German Research Foundation (DFG) [SFB 755]; European Commission [226716]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/226716/EU//ELISA"],["dc.relation.issn","1473-0197"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.subject.mesh","Adhesives"],["dc.subject.mesh","Adsorption"],["dc.subject.mesh","Finite Element Analysis"],["dc.subject.mesh","Fluorescein"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Microfluidic Analytical Techniques"],["dc.subject.mesh","Recombinant Proteins"],["dc.subject.mesh","Scattering, Small Angle"],["dc.subject.mesh","Vimentin"],["dc.subject.mesh","X-Ray Diffraction"],["dc.title","Dynamics of intermediate filament assembly followed in micro-flow by small angle X-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]