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化学计量比控制着缔合蛋白液滴的动力学。

Stoichiometry Controls the Dynamics of Liquid Condensates of Associative Proteins.

机构信息

Center for the Physics of Biological Function, Princeton University, Princeton, New Jersey 08544, USA.

Aix Marseille Univ, CNRS, CINAM, Turing Center for Living Systems, Marseille, France.

出版信息

Phys Rev Lett. 2022 Jan 21;128(3):038102. doi: 10.1103/PhysRevLett.128.038102.

DOI:10.1103/PhysRevLett.128.038102
PMID:35119898
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10497325/
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.

摘要

具有强互补相互作用的多价缔合蛋白在细胞内液滴相分离中起着至关重要的作用。我们通过标度分析和分子动力学研究了由两种互补蛋白组成的这种“键网络”凝聚物的内部动力学。我们发现,当化学计量平衡时,由于键断裂后替代结合伴侣的缺乏,弛豫会显著减慢。这种微观上的减速强烈影响了体扩散系数、粘度和混合,这为实验验证这一预测提供了一种手段。

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Protein condensates as aging Maxwell fluids.蛋白质凝聚物作为老化的麦克斯韦流体。
Proc Natl Acad Sci U S A. 2025 Jun 10;122(23):e2424135122. doi: 10.1073/pnas.2424135122. Epub 2025 Jun 2.
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