Avellaneda Mario J, Koers Eline J, Naqvi Mohsin M, Tans Sander J
AMOLF institute, Science Park 104, 1098XG Amsterdam, The Netherlands.
Protein Sci. 2017 Jul;26(7):1291-1302. doi: 10.1002/pro.3161. Epub 2017 Apr 20.
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the interactions between chaperones and their many clients, as well as the dynamics and heterogeneity of chaperone conformations and the folding process itself. While troublesome for traditional bulk techniques, these properties make an excellent case for the use of single-molecule approaches. In this review, we will discuss how force spectroscopy, fluorescence microscopy, FCS, and FRET methods are starting to zoom in on this intriguing and diverse molecular toolbox that is of direct importance for protein quality control in cells, as well as numerous degenerative conditions that depend on it.
众所周知，蛋白质折叠由一类名为伴侣蛋白的特殊蛋白质进行监督。然而，由于多种原因，这些分子机器的核心作用模式一直难以捉摸，这些原因包括伴侣蛋白与其众多底物之间相互作用的混杂性质，以及伴侣蛋白构象和折叠过程本身的动态性和异质性。虽然这些特性给传统的整体技术带来了麻烦，但却为单分子方法的应用提供了绝佳案例。在这篇综述中，我们将讨论力谱、荧光显微镜、荧光相关光谱和荧光共振能量转移方法如何开始聚焦于这个有趣且多样的分子工具箱，它对于细胞中的蛋白质质量控制以及许多依赖于它的退行性疾病具有直接重要性。
