Abstract
Multivalent associative proteins with strong complementary interactions play a crucial role in phase separation of intracellular liquid condensates. We study the internal dynamics of such "bond-network" condensates comprised of two complementary proteins via scaling analysis and molecular dynamics. We find that when stoichiometry is balanced, relaxation slows down dramatically due to a scarcity of alternative partners following a bond break. This microscopic slow-down strongly affects the bulk diffusivity, viscosity and mixing, which provides a means to experimentally test our predictions.
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