Many cellular processes rely on striking spatial patterns of proteins that constantly assemble and disassemble on membranes. In our new study, published in Nature Physics, we show that these active protein patterns can behave like foams and multicomponent liquid mixtures, even though there are no mechanical forces between the molecules. We introduce the concepts of “Turing mixtures” and “Turing foams” and develop a theory that predicts how their interface geometry and typical length scale are selected.
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A new PNAS study reveals "delay-facilitated assembly"—a counter-intuitive mechanism where slow exchange between reaction compartments significantly outperforms fast exchange. By turning the "reservoir" into a control knob, this approach maximizes yield and minimizes time, offering a blueprint for building reliable synthetic systems that mimic nature’s efficiency.
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