Stoichiometry Controls the Dynamics of Liquid Condensates of Associative Proteins
Pierre Ronceray, Yaojun Zhang, Xichong Liu, Ned S. Wingreen
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 comprising 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 binding partners following bond breakage. This microscopic slow-down strongly affects the bulk diffusivity, viscosity, and mixing, which provides a means to experimentally test this prediction.
Topics & Concepts
StoichiometryChemical physicsAssociative propertyDynamics (music)Relaxation (psychology)ScalingMolecular dynamicsPhase (matter)ChemistryProtein dynamicsPhysicsMaterials scienceBiophysicsLiquid phaseLiquid liquidProtein–protein interactionMoleculeIntracellularBiological systemStatistical physicsPlasma protein bindingProtein structureComponent (thermodynamics)AgrégationThermodynamicsMolecular physicsBiomoleculeRNA Research and SplicingProtein Structure and DynamicsLipid Membrane Structure and Behavior