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arXiv · 1106.5643

Monodisperse domains by proteolytic control of the coarsening instability

Julien Derr·Andrew Rutenberg
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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 novel 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 pseudo-pilus length control in the general secretion pathway of bacteria.

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Julien Derr, Andrew Rutenberg. 2011-06-28. Monodisperse domains by proteolytic control of the coarsening instability. https://doi.org/10.1103/physreve.84.011928

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