高分子拥挤和内在无序的蛋白质:一个高分子物理学的观点

IF 3.1 Q2 CHEMISTRY, MULTIDISCIPLINARY
Jasmine Cubuk, Dr. Andrea Soranno
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引用次数: 13

摘要

细胞是一个拥挤的环境,其中可用空间的相关部分被蛋白质、核酸和代谢物所占据。在这里,我们讨论了最近在拥挤效应对内在无序蛋白质的理解的进展。与结构蛋白质不同,这些蛋白质不采用稳定的三维结构,在溶液中保持灵活和动态。聚合物和胶体的物理学为解释拥挤如何调节无序蛋白质的构象、动力学和相互作用提供了一个框架。Flory-Huggins模型能够根据耗竭相互作用来合理化拥挤因子引起的不同程度的压实。同样的相互作用调节无序蛋白质在拥挤环境中的扩散,以及与配体相互作用时的结合和解离率。总之,这一理论框架为解释细胞环境对无序蛋白质的影响提供了新的见解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective

Macromolecular Crowding and Intrinsically Disordered Proteins: A Polymer Physics Perspective

The cell is a crowded environment where a relevant fraction of the available space is occupied by proteins, nucleic acids, and metabolites. Here we discuss recent advancements in the understanding of crowding effects on intrinsically disordered proteins. Differently from their structured counterparts, these proteins do not adopt a stable three-dimensional structure and remain flexible and dynamic in solution. The physics of polymers and colloids provides a framework to interpret how crowding modulates conformations, dynamics, and interactions of disordered proteins. Flory-Huggins models enable rationalizing the different degree of compaction induced by crowding agents in terms of depletion interactions. The same interactions modulate the diffusion of the disordered proteins in a crowded milieu and the association and dissociation rates when interacting with a ligand. Altogether, this theoretical framework provides new insights into the interpretation of the effects of the cellular environment on disordered proteins.

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