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Monodisperse domains by proteolytic control of the coarsening instability

dc.contributor.authorDerr, Julienen_US
dc.contributor.authorRutenberg, Andrew D.en_US
dc.date.accessioned2013-06-19T17:25:28Z
dc.date.available2013-06-19T17:25:28Z
dc.date.issued2011en_US
dc.description.abstractThe coarsening instability typically disrupts steady-state cluster-size distributions. We show that degradation coupled to the cluster size, such as arising from biological proteolysis, leads to a fixed-point cluster size. Stochastic evaporative and condensative fluxes determine the width of the fixed-point size distribution. At the fixed point, we show how the peak size and width depend on number, interactions, and proteolytic rate. This proteolytic size-control mechanism is consistent with the phenomenology of pseudopilus length control in the general secretion pathway of bacteria. 2011 American Physical Society.en_US
dc.identifier.citationDerr, Julien, and Andrew D. Rutenberg. 2011. "Monodisperse domains by proteolytic control of the coarsening instability." Physical Review E - Statistical, Nonlinear, and Soft Matter Physics 84(1).en_US
dc.identifier.issn15393755en_US
dc.identifier.issue1en_US
dc.identifier.startpageen_US
dc.identifier.urihttp://dx.doi.org/10.1103/PhysRevE.84.011928en_US
dc.identifier.urihttp://hdl.handle.net/10222/24838
dc.identifier.volume84en_US
dc.publisherAmerican Physical Societyen_US
dc.relation.ispartofPhysical Review E - Statistical, Nonlinear, and Soft Matter Physicsen_US
dc.subjectSize distributionen_US
dc.titleMonodisperse domains by proteolytic control of the coarsening instabilityen_US
dc.typearticleen_US

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