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Issue 40, 2014
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Early amyloid β-protein aggregation precedes conformational change

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Abstract

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.

Graphical abstract: Early amyloid β-protein aggregation precedes conformational change

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Publication details

The article was received on 14 Nov 2013, accepted on 09 Jan 2014 and first published on 15 Jan 2014


Article type: Communication
DOI: 10.1039/C3CC48704K
Citation: Chem. Commun., 2014,50, 5373-5375
  • Open access: Creative Commons BY license
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    Early amyloid β-protein aggregation precedes conformational change

    B. Barz, O. O. Olubiyi and B. Strodel, Chem. Commun., 2014, 50, 5373
    DOI: 10.1039/C3CC48704K

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