Early amyloid β-protein aggregation precedes conformational change.
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.
Forschungszentrum Jülich GmbH, Institute of Complex Systems: Structural Biochemistry (ICS-6), 52425 Jülich, Germany. b.strodel@fz-juelich.de.
Bogdan
B
Barz
Olujide O
OO
Olubiyi
Birgit
B
Strodel
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization
D016229:Amyloid beta-Peptides