Journal
PHYSICAL REVIEW LETTERS
Volume 128, Issue 3, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.128.038102
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Funding
- NSF, through the Center for the Physics of Biological Function [PHY-1734030]
- NIH [R01 GM140032]
- Susan and John Diekman '65 Genomics Faculty Support Fund through the Lewis-Sigler Institute of Integrative Genomics at Princeton University
- Princeton Biomolecular Condensate Program
- Investissements d'Avenir French Government program [ANR16-CONV-0001]
- Excellence Initiative of Aix-Marseille University-A*MIDEX
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Multivalent associative proteins are essential for phase separation in intracellular liquid condensates. This study investigates the internal dynamics of bond-network condensates composed of two complementary proteins through scaling analysis and molecular dynamics. The findings reveal that when the stoichiometry is balanced, relaxation significantly slows down due to a lack of alternative binding partners, which strongly influences bulk diffusivity, viscosity, and mixing. This provides an experimental means to test the prediction.
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.
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