Effect of Grafting on Aggregation of Intrinsically Disordered Proteins

被引：4
|
作者：
Osmanovic, Dino [1 ,2 ]
Rabin, Yitzhak [2 ]
机构：
[1] MIT, Dept Phys Living Syst, 77 Massachusetts Ave, Cambridge, MA 02139 USA
[2] Bar Ilan Univ, Dept Phys, Ramat Gan, Israel
来源：
BIOPHYSICAL JOURNAL | 2018年 / 114卷 / 03期
基金：
以色列科学基金会;
关键词：
NUCLEAR-PORE COMPLEX; REPEAT REGIONS; NEUROFILAMENTS; NUCLEOPORINS; POLYMERS; DYNAMICS;
D O I：
10.1016/j.bpj.2017.08.062
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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.
引用
收藏
页码：534 / 538
页数：5
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