Elastin-like proteins (ELPs) undergo reversible coacervation above a certain transition temperature. The thermodynamic analysis of temperature-dependent circular dichroism of ELPs of different chain-length revealed that this is preceded by a step-by-step increase of β-turn structure. When a certain threshold is reached, phase separation occurs. The conformational ratio in the assembled protein particles still corresponds to this threshold.

中文翻译：

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本质无序-有序蛋白质模型相分离过程中的动态结构变化和热力学

弹性蛋白样蛋白 (ELP) 在高于某个转变温度时会发生可逆凝聚。对不同链长 ELP 的温度相关圆二色性的热力学分析表明，在此之前，β-转角结构逐步增加。当达到某个阈值时，就会发生相分离。组装的蛋白质颗粒中的构象比仍然对应于这个阈值。