Conformational plasticity of small Hsps (A06)

小热休克蛋白（sHsps）是一种分子伴侣，对蛋白质毒性应激起第一反应。sHsps的一个显著特征是它们是相互转化的低聚物的动态集合，这与它们的伴侣活性直接相关。在之前的工作中，我们讨论了sHsps的结构和机制方面，包括在构象水平上控制其活性的调控触发器。在未来的工作中，我们将扩大sHsp的构象动力学研究，重点关注其寡聚结构，sHsp的N端区域和底物识别，以及活性调节的机制原理。

Small heat shock proteins (sHsps) are molecular chaperones which act as a first response to proteotoxic stress. A striking feature of sHsps is their existence as dynamic ensembles of interconverting oligomers which is directly linked to their chaperone activity. In previous work, we addressed structural and mechanistic aspects of sHsps including regulatory triggers that control their activity on the conformational level. In future work, we will expand our studies on the conformational dynamics regulating sHsp with a focus on their oligomeric structures, the N terminal region of sHsps and substrate recognition, and mechanistic principles of activity regulation.