Cytoskeleton proteins, such as actin filaments, microtubules, intermediate filaments, play an important role in the functioning of biological systems. The cellular functions of these rigid filament proteins are defined by their growth processes. A theoretical analysis of the growth dynamics of cytoskeleton proteins is presented from the point of view of different scales. It is argued that simple phenomenological models cannot reasonably describe the polymerization processes, while the atomic scale analysis is still technically not feasible. We present a mesoscopic theoretical approach that takes into account the structure and geometry of the growing proteins, chemical processes and chemical interactions between the subunits. The method is successfully applied to explain and to analyze the experimental observations. It is shown that chemical processes on the microscopic level might lead to large macroscopic fluctuations in cytoskeleton proteins
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