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Intrinsically disordered proteins access a range of hysteretic phase separation behaviors

机译:本质上无序的蛋白质具有一系列迟滞相分离行为

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摘要

The phase separation behavior of intrinsically disordered proteins (IDPs) is thought of as analogous to that of polymers that undergo equilibrium lower or upper critical solution temperature (LCST and UCST, respectively) phase transition. This view, however, ignores possible nonequilibrium properties of protein assemblies. Here, by studying IDP polymers (IDPPs) composed of repeat motifs that encode LCST or UCST phase behavior, we discovered that IDPs can access a wide spectrum of nonequilibrium, hysteretic phase behaviors. Experimentally and through simulations, we show that hysteresis in IDPPs is tunable and that it emerges through increasingly stable interchain interactions in the insoluble phase. To explore the utility of hysteretic IDPPs, we engineer self-assembling nanostructures with tunable stability. These findings shine light on the rich phase separation behavior of IDPs and illustrate hysteresis as a design parameter to program nonequilibrium phase behavior in self-assembling materials.
机译:固有无序蛋白(IDP)的相分离行为被认为与经历平衡的较低或较高的临界溶液温度(分别为LCST和UCST)相变的聚合物的相分离行为类似。然而,这种观点忽略了蛋白质组装体可能的非平衡性质。在这里,通过研究由编码LCST或UCST相行为的重复基序组成的IDP聚合物(IDPP),我们发现IDP可以访问广泛的非平衡,迟滞相行为。通过实验和仿真,我们表明IDPP中的磁滞是可调的,并且它通过不溶相中日益稳定的链间相互作用而出现。为了探索迟滞IDPP的实用性,我们设计了具有可调稳定性的自组装纳米结构。这些发现为IDP的富相分离行为提供了亮点,并说明了磁滞作为一种设计参数,可对自组装材料中的非平衡相行为进行编程。

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