Stoichiometry Controls the Dynamics of Liquid Condensates of Associative Proteins.

TitleStoichiometry Controls the Dynamics of Liquid Condensates of Associative Proteins.
Publication TypeJournal Article
Year of Publication2022
AuthorsRonceray, P, Zhang, Y, Liu, X, Wingreen, NS
JournalPhys Rev Lett
Volume128
Issue3
Pagination038102
Date Published2022 Jan 21
ISSN1079-7114
KeywordsBiophysical Phenomena, Models, Chemical, Molecular Dynamics Simulation, Proteins, Viscosity
Abstract

<p>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.</p>

DOI10.1103/PhysRevLett.128.038102
Alternate JournalPhys Rev Lett
PubMed ID35119898