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The Chylla–Haase polymerization reactor is widely accepted as a benchmark process for the evaluation of control strategies for batch reactors. In this contribution a control concept based on Exact I/O-Linearization is proposed and compared to a conventional cascade control structure. In order to adapt the exact linearization control strategy to various polymerization products and batch conditions, an advanced probabilistic inference algorithm (Sigma-Point Kalman Filter) is applied and investigated. Sigma-Point Kalman Filters have the major improvement of simplified implementation compared to local linearization methods (i.e. Extended Kalman Filter) because no analytical Jacobians are required. Stochastic simulation studies are introduced and show the effectiveness, accuracy and benefit of the control concept. Within several scenarios a satisfying robustness against structural errors in the underlying model equations for the nonlinear control law and the inference algorithm is demonstrated. Furthermore it is pointed out, that with little effort in reassembling the plant design, control performance can be improved significantly.
Many different cell types are able to migrate by formation of a thin actin-based cytoskeletal extension. Recently, it became evident that this extension consists of two distinct substructures, designated lamellipodium and lamellum, which differ significantly in their kinetic and kinematic properties as well as their biochemical composition. We developed a stochastic two-dimensional computer simulation that includes chemical reaction kinetics, G-actin diffusion, and filament transport to investigate the formation of growing actin networks in migrating cells. Model parameters were chosen based on experimental data or theoretical considerations. In this work, we demonstrate the system's ability to form two distinct networks by self-organization. We found a characteristic transition in mean filament length as well as a distinct maximum in depolymerization flux, both within the first 1-2 microm. The separation into two distinct substructures was found to be extremely robust with respect to initial conditions and variation of model parameters. We quantitatively investigated the complex interplay between ADF/cofilin and tropomyosin and propose a plausible mechanism that leads to spatial separation of, respectively, ADF/cofilin- or tropomyosin-dominated compartments. Tropomyosin was found to play an important role in stabilizing the lamellar actin network. Furthermore, the influence of filament severing and annealing on the network properties is explored, and simulation data are compared to existing experimental data.