Early amyloid β-protein aggregation precedes conformational change.
نویسندگان
چکیده
The aggregation of amyloid-β protein (1-42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers without significant changes in the internal structure of individual proteins. The aggregation process is characterized in terms of transition networks.
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ورودعنوان ژورنال:
- Chemical communications
دوره 50 40 شماره
صفحات -
تاریخ انتشار 2014