%0 Journal Article
%A Barz, Bogdan
%A Olubiyi, Olujide O.
%A Strodel, Birgit
%T Early amyloid β-protein aggregation precedes conformational change
%J Chemical communications
%V 50
%N 40
%@ 1364-548X
%C Cambridge
%I Soc.
%M FZJ-2014-00974
%P 5373-5375
%D 2014
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000335011200066
%$ pmid:24471163
%R 10.1039/c3cc48704k
%U https://juser.fz-juelich.de/record/150941