Phase transitions and structure analysis in wild-type, A30P, E46K, and A53T mutants of α-synuclein

被引：0
|
作者：
Mark A. Healey
Michael T. Woodside
Jack A. Tuszynski
机构：
[1] University of Alberta,Department of Physics
[2] National Research Council,National Institute for Nanotechnology
[3] University of Alberta,Department of Oncology
来源：
European Biophysics Journal | 2016年 / 45卷
关键词：
Intrinsically disordered protein; α-Synuclein; Parkinson’s disease; Monte Carlo simulations; Phase transitions; Mutations;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
α-Synuclein has been implicated in the development of neural plaques in Parkinson’s Disease and Lewy-Body Dementia. This paper reports on the structural phase change behavior exhibited over a relevant range of temperatures in canonical protein Monte Carlo simulations for wild-type α-synuclein and three of its familial variants. We performed and analyzed these simulations to determine residue occupancy variations above and below this phase transition. From this analysis, we found regions above the phase transition temperature that consistently exhibited increased propensity for formation of long-chain beta-sheets, suggesting a possible role in α-synuclein aggregation.
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页码：355 / 364
页数：9
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