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.

References in corpus (1)

• Generalized models for bond percolation transitions of associative polymers

Cited by in corpus (2)

• Rheology and Viscoelasticity of Proteins and Nucleic Acids Condensates
• Thermodynamically Consistent Phase-Field Theory Including Nearest-Neighbor Pair Correlations Explains Failure of Mean-Field Reasoning