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. 2011 American Physical Society.
Citation
Derr, 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).