Department of Structural Biology, Weizmann Institute of Science, Herzl St. 234, 76100 Rehovot, Israel.
Methods Appl Fluoresc. 2016 Nov 17;4(4):042003. doi: 10.1088/2050-6120/4/4/042003.
Understanding protein folding and the functional properties of intrinsically disordered proteins (IDPs) requires detailed knowledge of the forces that act in polypeptide chains. These forces determine the dimensions and dynamics of unfolded and disordered proteins and have been suggested to impact processes such as the coupled binding and folding of IDPs, or the rate of protein folding reactions. Much of the progress in understanding the physical and chemical properties of unfolded and intrinsically disordered polypeptide chains has been made possible by the recent developments in single-molecule fluorescence techniques. However, the interpretation of the experimental results requires concepts from polymer physics in order to be understood. Here, I review some of the theories used to describe the dimensions of unfolded polypeptide chains under varying solvent conditions together with their more recent application to experimental data.
理解蛋白质折叠和无规卷曲蛋白质（IDPs）的功能特性需要详细了解作用于多肽链的力。这些力决定了未折叠和无规卷曲蛋白质的尺寸和动力学，并被认为会影响 IDPs 的结合和折叠等过程，或者蛋白质折叠反应的速度。理解未折叠和无规卷曲多肽链的物理和化学性质的大部分进展得益于单分子荧光技术的最新发展。然而，为了理解实验结果，需要使用聚合物物理的概念。在这里，我回顾了一些用于描述在不同溶剂条件下展开的多肽链的尺寸的理论，以及它们最近在实验数据中的应用。
