Abstract
Aggregation of amyloid-β (Aβ42) protein is one hallmark of Alzheimer's disease, and the conformations of the smallest Aβ42 oligomers are largely unknown. Here, we explore the application of the deep learning AlphaFold2 method to the structure determination of Aβ42 monomers up to hexamers. The results shed light on the early Aβ42 aggregation steps in the bulk solution.
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