Many fundamental cellular processes are spatially regulated by self-organized protein patterns, which are often based on nucleotide-binding proteins that switch their nucleotide state upon interaction with a second, activating protein. For reliable function, these protein patterns must be robust against parameter changes, although the basis for such robustness is generally elusive. Here, we take a combined theoretical and experimental approach to the E. coli Min system, a paradigmatic system for protein self-organization.
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