Journal Article

FZJ-2014-00974

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Early amyloid β-protein aggregation precedes conformational change

Barz, B.FZJ* ; Olubiyi, O. O. ; Strodel, B. (Corresponding author)FZJ*

2014
Soc. Cambridge

This record in other databases:      

Please use a persistent id in citations: http://hdl.handle.net/2128/22904  doi:10.1039/c3cc48704k

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2014

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Database coverage:
; ; ; Allianz-Lizenz / DFG ; Current Contents - Social and Behavioral Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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