Aggregation of β-amyloid fragments
Copyright policy )Aggregation of β-amyloid fragments
The authors study the folding and aggregation of six chains of the β-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 β sheets below a crossover temperature Tx≈420K. 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.
- Forschungszentrum Jülich Germany
- Michigan Technological University United States
- Helmholtz Association of German Research Centres Germany
- John von Neumann Institute for Computing Germany
Models, Molecular, Protein Folding, Amyloid beta-Peptides, Binding Sites, info:eu-repo/classification/ddc/540, Amyloid beta-Peptides: chemistry, Protein Conformation, Temperature, Multiprotein Complexes: chemistry, amyloid beta-protein (16-22), Amyloid beta-Peptides: ultrastructure, Peptide Fragments, J, Multiprotein Complexes: ultrastructure, Peptide Fragments: chemistry, Models, Chemical, Multiprotein Complexes, Computer Simulation, Peptide Fragments: ultrastructure, Dimerization, Monte Carlo Method, Protein Binding
Models, Molecular, Protein Folding, Amyloid beta-Peptides, Binding Sites, info:eu-repo/classification/ddc/540, Amyloid beta-Peptides: chemistry, Protein Conformation, Temperature, Multiprotein Complexes: chemistry, amyloid beta-protein (16-22), Amyloid beta-Peptides: ultrastructure, Peptide Fragments, J, Multiprotein Complexes: ultrastructure, Peptide Fragments: chemistry, Models, Chemical, Multiprotein Complexes, Computer Simulation, Peptide Fragments: ultrastructure, Dimerization, Monte Carlo Method, Protein Binding
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