Journal Article

PreJuSER-55426

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Aggregation of Beta-Amyloid Fragments

Meinke, J.FZJ* ; Hansmann, U.FZJ*

2007
American Institute of Physics Melville, NY

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Please use a persistent id in citations: http://hdl.handle.net/2128/19093  doi:10.1063/1.2423013

Abstract: The authors study the folding and aggregation of six chains of the beta-amyloid fragment 16-22 using Monte Carlo simulations. While the isolated fragment prefers a helical form at room temperature, in the system of six interacting fragments one observes both parallel and antiparallel beta sheets below a crossover temperature T(x) approximately equal to 420 K. The antiparallel sheets have lower energy and are therefore more stable. Above the nucleation temperature the aggregate quickly dissolves into widely separated, weakly interacting chains.

Keyword(s): Amyloid beta-Peptides: chemistry (MeSH) ; Amyloid beta-Peptides: ultrastructure (MeSH) ; Binding Sites (MeSH) ; Computer Simulation (MeSH) ; Dimerization (MeSH) ; Models, Chemical (MeSH) ; Models, Molecular (MeSH) ; Monte Carlo Method (MeSH) ; Multiprotein Complexes: chemistry (MeSH) ; Multiprotein Complexes: ultrastructure (MeSH) ; Peptide Fragments: chemistry (MeSH) ; Peptide Fragments: ultrastructure (MeSH) ; Protein Binding (MeSH) ; Protein Conformation (MeSH) ; Protein Folding (MeSH) ; Temperature (MeSH) ; Amyloid beta-Peptides ; Multiprotein Complexes ; Peptide Fragments ; amyloid beta-protein (16-22) ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. John von Neumann - Institut für Computing (NIC)

Research Program(s):

1. Scientific Computing (P41)

Appears in the scientific report 2007

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Database coverage:

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