Issue 40, 2014

Early amyloid β-protein aggregation precedes conformational change

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

Supplementary files

Article information

Article type
Communication
Submitted
14 Nov. 2013
Accepted
09 Janv. 2014
First published
15 Janv. 2014
This article is Open Access
Creative Commons BY license

Chem. Commun., 2014,50, 5373-5375

Author version available

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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