title: Computational studies of protein aggregation: methods and applications.
abstract: Protein aggregation involves the self-assembly of normally soluble proteins into large supramolecular assemblies. The typical end product of aggregation is the amyloid fibril, an extended structure enriched in β-sheet content. The aggregation process has been linked to a number of diseases, most notably Alzheimer's disease, but fibril formation can also play a functional role in certain organisms. This review focuses on theoretical studies of the process of fibril formation, with an emphasis on the computational models and methods commonly used to tackle this problem.
authors: Department of Physics and.
authors: Alex
authors: A
authors: Morriss-Andrews
authors: Joan-Emma
authors: JE
authors: Shea
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D003198:Computer Simulation; D006801:Humans; D008958:Models, Molecular; D066329:Protein Aggregates; D066263:Protein Aggregation, Pathological / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D000682:Amyloid; D066329:Protein Aggregates
keywords: amyloid fibrils; coarse-grained models; enhanced sampling methods; molecular dynamics simulations; replica exchange molecular dynamics; systematic coarse graining