Department of Biochemistry and Molecular Biophysics, Center for the Science and Engineering of Living Systems, Washington University in St Louis, St Louis, MO, 63130, USA.
Arch Biochem Biophys. 2020 May 30;685:108305. doi: 10.1016/j.abb.2020.108305. Epub 2020 Mar 5.
Intrinsically disordered proteins do not adopt well-defined structures, yet they still play functional roles in many different aspects of biology. Their lack of stable conformations poses new challenges to the quantitative description and understanding of their processes, since they cannot be formulated within the classical terms of structural biology. Polymer physics is emerging as a powerful language to identify, describe, and quantify the molecular determinants of the disordered conformational ensemble. Here, I will review the application of key-concepts of polymer theories to intrinsically disordered proteins, with a particular focus on the role played by residue-residue and residue-solvent interactions in modulating conformational transitions in the disordered structural ensemble.
无规蛋白不采用明确的结构，但它们在生物学的许多不同方面仍然发挥功能作用。它们缺乏稳定的构象，这给定量描述和理解它们的过程带来了新的挑战，因为它们不能用结构生物学的经典术语来描述。聚合物物理正在成为一种强大的语言，可以识别、描述和量化无规构象的分子决定因素。在这里，我将回顾聚合物理论的关键概念在无规蛋白中的应用，特别关注残基-残基和残基-溶剂相互作用在调节无规结构构象转变中的作用。
