Center for High Performance Simulations, North Carolina State University, Raleigh, North Carolina 27695, USA.
Proteins. 2011 Mar;79(3):937-46. doi: 10.1002/prot.22935. Epub 2011 Jan 3.
The α-sheet has been speculated to play a role as a toxic conformer in amyloid diseases. However, except for relatively short fragments, its detection has remained elusive. Here, we present molecular dynamics simulations that support the existence of the α-sheet as a stable, metastable, or long-lived secondary structure in polyglutamine and, to a lesser extent, in polyasparagine aggregates.
α-折叠结构被推测在淀粉样疾病中作为一种毒性构象发挥作用。然而，除了相对较短的片段之外，其检测仍然难以捉摸。在这里，我们提供了分子动力学模拟结果，支持α-折叠结构作为多聚谷氨酰胺（polyglutamine）聚合体中一种稳定、亚稳定或长寿命的二级结构存在，在一定程度上也存在于多聚天冬酰胺（polyasparagine）聚合体中。
