Assays for studying nucleated aggregation of polyglutamine proteins

被引：27
|
作者：
Jayaraman, Murali
Thakur, Ashwani K.
Kar, Karunakar
Kodali, Ravindra
Wetzel, Ronald [1 ]
机构：
[1] Dept Biol Struct, Pittsburgh, PA 15260 USA
来源：
METHODS | 2011年 / 53卷 / 03期
关键词：
Kinetics; Thioflavin T; Seeding; Amyloid; Oligomer; Fluorescence; HUNTINGTONS-DISEASE; EXPANSION; EXCHANGE; BINDING; THERMODYNAMICS; PROTOFIBRILS; CONFORMATION; MECHANISM; FEATURES;
D O I：
10.1016/j.ymeth.2011.01.001
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The aggregation of polyglutamine containing protein sequences is implicated in a family of familial neurodegenerative diseases, the expanded CAG repeat diseases. While the cellular aggregation process undoubtedly depends on the flux and local environment of these proteins, their intrinsic physical properties and folding/aggregation propensities must also contribute to their cellular behavior. Here we describe a series of methods for determining mechanistic details of the spontaneous aggregation of polyQ-containing sequences, including the identification and structural examination of aggregation intermediates. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码：246 / 254
页数：9
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