Heussinger, Claus

[["dc.bibliographiccitation.artnumber","095029"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","New Journal of Physics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.affiliation","Heussinger, C;"],["dc.contributor.author","Heussinger, Claus"],["dc.date.accessioned","2018-11-07T09:05:43Z"],["dc.date.available","2018-11-07T09:05:43Z"],["dc.date.issued","2012"],["dc.date.updated","2022-02-10T06:27:00Z"],["dc.description.abstract","The mechanical properties of cells are dominated by the cytoskeleton, an interconnected network of long elastic filaments. The connections between the filaments are provided by crosslinking proteins, which constitute, next to the filaments, the second important mechanical element of the network. An important aspect of cytoskeletal assemblies is their dynamic nature, which allows remodeling in response to external cues. The reversible nature of crosslink binding is an important mechanism that underlies these dynamical processes. Here, we develop a theoretical model that provides us insight into how the mechanical properties of cytoskeletal networks may depend on their underlying constituting elements. We incorporate three important ingredients: non-affine filament deformations in response to network strain; the interplay between filament and crosslink mechanical properties; and reversible crosslink (un) binding in response to the imposed stress. With this we are able to self-consistently calculate the nonlinear modulus of the network as a function of deformation amplitude and crosslink as well as filament stiffnesses. During loading, crosslink unbinding processes lead to a relaxation of stress and therefore to a reduction of the network modulus and eventually to network failure, when all crosslinks are unbound. This softening due to crosslink unbinding generically competes with an inherent stiffening response, which may be due to either filament or crosslink nonlinear elasticity."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2012"],["dc.identifier.doi","10.1088/1367-2630/14/9/095029"],["dc.identifier.eissn","1367-2630"],["dc.identifier.isi","000309395100001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25390"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","IOP Publishing"],["dc.relation.issn","1367-2630"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-sa/3.0/"],["dc.title","Stress relaxation through crosslink unbinding in cytoskeletal networks"],["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.artnumber","083035"],["dc.bibliographiccitation.journal","New Journal of Physics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Amuasi, H. E."],["dc.contributor.author","Heussinger, Claus"],["dc.contributor.author","Vink, Richard L. C."],["dc.contributor.author","Zippelius, Annette"],["dc.date.accessioned","2018-11-07T09:53:19Z"],["dc.date.available","2018-11-07T09:53:19Z"],["dc.date.issued","2015"],["dc.description.abstract","We simulate randomly crosslinked networks of biopolymers, characterizing linear and nonlinear elasticity under different loading conditions (uniaxial extension, simple shear, and pure shear). Under uniaxial extension, and upon entering the nonlinear regime, the network switches from a dilatant to contractile response. Analogously, under isochoric conditions (pure shear), the normal stresses change their sign. Both effects are readily explained with a generic weakly nonlinear elasticity theory. The elastic moduli display an intermediate super-stiffening regime, where moduli increase much stronger with applied stress sigma than predicted by the force-extension relation of a single wormlike-chain (G(wlc) similar to sigma(3/2)). We interpret this super-stiffening regime in terms of the reorientation of filaments with the maximum tensile direction of the deformation field. A simple model for the reorientation response gives an exponential stiffening, G similar to e(sigma), in qualitative agreement with our data. The heterogeneous, anisotropic structure of the network is reflected in correspondingly heterogeneous and anisotropic elastic properties. We provide a coarse-graining scheme to quantify the local anisotropy, the fluctuations of the elastic moduli, and the local stresses as a function of coarse-graining length. Heterogeneities of the elastic moduli are strongly correlated with the local density and increase with applied strain."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1088/1367-2630/17/8/083035"],["dc.identifier.isi","000360956600003"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36308"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Iop Publishing Ltd"],["dc.relation.issn","1367-2630"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 3.0"],["dc.title","Nonlinear and heterogeneous elasticity of multiply-crosslinked biopolymer networks"],["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","4806"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","4812"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Moebius, Ronny"],["dc.contributor.author","Heussinger, Claus"],["dc.date.accessioned","2018-11-07T09:46:03Z"],["dc.date.available","2018-11-07T09:46:03Z"],["dc.date.issued","2014"],["dc.description.abstract","We use computer simulations to study highly dense systems of granular particles that are driven by oscillating forces. We implement different dissipation mechanisms that are used to extract the injected energy. In particular, the action of a simple local Stokes' drag is compared with non-linear and history-dependent frictional forces that act either between particle pairs or between particles and an external container wall. The Stokes' drag leads to particle motion that is periodic with the driving force, even at high densities around close packing where particles undergo frequent collisions. With the introduction of inter-particle frictional forces this \"interacting absorbing state\" is destroyed and particles start to diffuse around. By reducing the density of the material we go through another transition to a \"non-interacting\" absorbing state, where particles independently follow the force-induced oscillations without collisions. In the system with particle-wall frictional interactions this transition has signs of a discontinuous phase transition. It is accompanied by a diverging relaxation time, but not by a vanishing order parameter, which rather jumps to zero at the transition."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft, Emmy Noether program [He 6322/1-1]"],["dc.identifier.doi","10.1039/c4sm00178h"],["dc.identifier.isi","000338123700006"],["dc.identifier.pmid","24838939"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11725"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34777"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 3.0"],["dc.title","(Ir)reversibility in dense granular systems driven by oscillating forces"],["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.artnumber","50"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","The European Physical Journal E"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Maier, M."],["dc.contributor.author","Mueller, K. W."],["dc.contributor.author","Heussinger, Claus"],["dc.contributor.author","Koehler, S."],["dc.contributor.author","Wall, W. A."],["dc.contributor.author","Bausch, A. R."],["dc.contributor.author","Lieleg, O."],["dc.date.accessioned","2018-11-07T09:57:02Z"],["dc.date.available","2018-11-07T09:57:02Z"],["dc.date.issued","2015"],["dc.description.abstract","Actin binding proteins ( ABPs) not only set the structure of actin filament assemblies but also mediate the frequency-dependent viscoelastic moduli of cross-linked and bundled actin networks. Point mutations in the actin binding domain of those ABPs can tune the association and dissociation dynamics of the actin/ABP bond and thus modulate the network mechanics both in the linear and non-linear response regime. We here demonstrate how the exchange of a single charged amino acid in the actin binding domain of the ABP fascin triggers such a modulation of the network rheology. Whereas the overall structure of the bundle networks is conserved, the transition point from strain-hardening to strain-weakening sensitively depends on the cross-linker off-rate and the applied shear rate. Our experimental results are consistent both with numerical simulations of a cross-linked bundle network and a theoretical description of the bundle network mechanics which is based on non-affine bending deformations and force-dependent cross-link dynamics."],["dc.identifier.doi","10.1140/epje/i2015-15050-3"],["dc.identifier.isi","000354960400001"],["dc.identifier.pmid","26004635"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11965"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37082"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1292-895X"],["dc.relation.issn","1292-8941"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 4.0"],["dc.title","A single charge in the actin binding domain of fascin can independently tune the linear and non-linear response of an actin bundle network"],["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"]]