The intriguing process of protein folding comprises discrete steps that stabilize the protein molecules in different conformations. The metastable state of protein is represented by specific conformational characteristics, which place the protein in a local free energy minimum state of the energy landscape. The native‐to‐metastable structural transitions are governed by transient or long‐lived thermodynamic and kinetic fluctuations of the intrinsic interactions of the protein molecules. Depiction of the structural and functional properties of metastable proteins is not only required to understand the complexity of folding patterns but also to comprehend the mechanisms of anomalous aggregation of different proteins. In this article, we review the properties of metastable proteins in context of their stability and capability of undergoing atypical aggregation in physiological conditions.

中文翻译：

---

蛋白质的亚稳态。


蛋白质折叠的有趣过程包括将蛋白质分子稳定在不同构象的离散步骤。蛋白质的亚稳态由特定的构象特征表示，这些特征使蛋白质处于能量景观的局部自由能最小状态。天然到亚稳态的结构转变受到蛋白质分子内在相互作用的瞬时或长期热力学和动力学波动的控制。描述亚稳态蛋白质的结构和功能特性不仅需要了解折叠模式的复杂性，而且还需要理解不同蛋白质异常聚集的机制。在本文中，我们回顾了亚稳态蛋白的稳定性和在生理条件下进行非典型聚集的能力的特性。