Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics

One of the earliest events in amyloid β-protein (Aβ) self-association is nucleation of Aβ monomer folding through formation of a turn at Gly25–Lys28. We report here the effects of structural changes at the center of the turn, Gly25-Ser26, on Aβ42 conformational dynamics and assembly. We used “click...

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Hlavní autoři: Roychaudhuri, Robin, Lomakin, Aleksey, Bernstein, Summer, Zheng, Xueyun, Condron, Margaret M., Benedek, George B., Bowers, Michael, Teplow, David B.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2014
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC4191920/
https://ncbi.nlm.nih.gov/pubmed/24735871
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2014.04.004
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