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 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.

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

References in corpus (3)

• Non-equilibrium raft-like membrane domains under continuous recycling
• Chirality and Equilibrium Biopolymer Bundles
• Packing defects and the width of biopolymer bundles