Protein conformational states-from intrinsically disordered ensembles to amyloids that underlie the self-templating, infectious properties of prion-like proteins-have attracted much attention. Here, we highlight the diversity, including differences in biophysical properties, that drive distinct biological functions and pathologies among self-templating proteins. Advances in chemical genomics, gene editing, and model systems now permit deconstruction of the complex interplay between these protein states and the host factors that react to them. These methods reveal that conformational switches modulate normal and abnormal information transfer and that intimate relationships exist between the intrinsic function of proteins and the deleterious consequences of their misfolding.

中文翻译：

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通过不同的蛋白质和蛋白质构象对生理和疾病状态的规范。

蛋白质构象状态-从本质上无序的合体到a蛋白样蛋白质的自模板性，传染性基础的淀粉样蛋白-引起了人们的极大关注。在这里，我们强调了多样性，包括生物物理特性的差异，这些差异在自我模板蛋白之间驱动着独特的生物学功能和病理。化学基因组学，基因编辑和模型系统的进步现在允许解构这些蛋白质状态和与其反应的宿主因子之间的复杂相互作用。这些方法揭示构象开关调节正常和异常的信息传递，并且蛋白质的内在功能与其错误折叠的有害后果之间存在密切的关系。