Stoichiometry Controls the Dynamics of Liquid Condensates of Associative Proteins
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.
Domains
Physics [physics]Origin | Files produced by the author(s) |
---|