Computational and Functional Genomics Group, Centre for DNA Fingerprinting and Diagnostics, Uppal, Hyderabad, Telangana, India.
Protein Sci. 2020 Jul;29(7):1559-1568. doi: 10.1002/pro.3859. Epub 2020 Apr 11.
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.
蛋白质折叠的有趣过程包括离散的步骤,这些步骤稳定了不同构象的蛋白质分子。蛋白质的亚稳定状态由特定的构象特征来表示,这些特征使蛋白质处于能量景观中的局部自由能最小值状态。天然到亚稳定的结构转变受蛋白质分子内在相互作用的瞬态或长寿命热力学和动力学波动的控制。描绘亚稳定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,还需要理解不同蛋白质异常聚集的机制。在本文中,我们将根据亚稳定蛋白质的稳定性及其在生理条件下发生非典型聚集的能力来综述它们的性质。