Department of Physics of Living Systems, MIT, Cambridge, Massachusetts; Department of Physics, Bar-Ilan University, Ramat-Gan, Israel.
Department of Physics, Bar-Ilan University, Ramat-Gan, Israel.
Biophys J. 2018 Feb 6;114(3):534-538. doi: 10.1016/j.bpj.2017.08.062. Epub 2018 Jan 31.
A significant part of the proteome is composed of intrinsically disordered proteins (IDPs). These proteins do not fold into a well-defined structure and behave like ordinary polymers. In this work, we consider IDPs that have the tendency to aggregate, model them as heteropolymers that contain a small number of associating monomers, and use computer simulations to compare the aggregation of such IDPs that are grafted to a surface or free in solution. We then discuss how such grafting may affect the analysis of in vitro experiments and could also be used to suppress harmful aggregation.
蛋白质组的很大一部分由固有无序蛋白质（IDP）组成。这些蛋白质不会折叠成明确的结构，而是表现得像普通聚合物一样。在这项工作中，我们考虑具有聚集倾向的 IDP，将它们建模为包含少量缔合单体的杂多聚物，并使用计算机模拟来比较这些 IDP 在表面接枝或在溶液中自由时的聚集。然后，我们讨论这种接枝如何影响体外实验的分析，以及如何用于抑制有害聚集。
