title: Monodisperse domains by proteolytic control of the coarsening instability.
abstract: The 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.
authors.affiliation: Department of Physics and Atmospheric Science, Dalhousie University, Halifax, Nova Scotia, Canada B3H 3J5. julien.derr@univ-paris-diderot.fr
authors.forename: Julien
authors.initials: J
authors.lastname: Derr
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Rutenberg
mesh_terms: D001419:Bacteria / Q000378:metabolism*; D018407:Bacterial Physiological Phenomena; D001703:Biophysics / Q000379:methods*; D002462:Cell Membrane / Q000378:metabolism; D016000:Cluster Analysis; D005407:Flagella / Q000378:metabolism; D008954:Models, Biological; D015233:Models, Statistical; D011336:Probability; D059748:Proteolysis; D013269:Stochastic Processes