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Physical basis of the disorder-order transition.
Archives of Biochemistry and Biophysics ( IF 3.8 ) Pub Date : 2020-03-05 , DOI: 10.1016/j.abb.2020.108305
Andrea Soranno 1
Affiliation  

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.

中文翻译:

无序转换的物理基础。

本质上无序的蛋白质没有采用明确定义的结构,但它们仍在生物学的许多不同方面发挥功能性作用。他们缺乏稳定的构象,对它们的过程进行定量描述和理解提出了新的挑战,因为它们不能用结构生物学的经典术语来表达。高分子物理学正在成为一种强大的语言,可以识别,描述和量化无序构象系综的分子决定因素。在这里,我将回顾聚合物理论的关键概念在本质上无序的蛋白质中的应用,特别关注残基-残基和残基-溶剂相互作用在调节无序结构体中构象转变中所起的作用。
更新日期:2020-03-05
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