Monodisperse domains by proteolytic control of the coarsening instability

Details Monodisperse domains by proteolytic control of the coarsening instability Monodisperse domains by proteolytic control of the coarsening instability

2011-06-28

arxiv.org/abs/1106.5643v1

Physics

Biological Physics

Physical Review E: Statistical, Nonlinear, and Soft Matter Physics (2011) in press

Scientific paper

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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