title: [Structure of amyloid fibrils].
abstract: Amyloid fibrils are structurally defined as fibrillar polypeptide aggregates with a characteristic cross-beta structure. Such fibrils can be formed by certain polypeptide sequences in the human body and by numerous polypeptide sequences in vitro. All amyloid fibrils possess a structural spine that is formed by a cross-beta structure. This structure is stabilized by hydrogen bonds between the polypeptide backbone. In recent years, various biophysical techniques, such as X-ray crystallography, solid state nuclear magnetic resonance spectroscopy and electron cryo-microscopy have provided insights into the structural organization of amyloid fibrils. This review presents an overview of important results obtained with these methods.
authors.affiliation: Leibniz-Institut für Altersforschung (Fritz-Lipmann-Institut), Jena, Deutschland.
authors.forename: J
authors.initials: J
authors.lastname: Meinhardt
authors.forename: M
authors.initials: M
authors.lastname: Fändrich
mesh_terms: D000544:Alzheimer Disease / Q000473:pathology; D000682:Amyloid / Q000032:analysis* / Q000648:ultrastructure; D000686:Amyloidosis / Q000473:pathology*; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D019636:Neurodegenerative Diseases / Q000473:pathology; D010455:Peptides / Q000032:analysis; D017096:Prion Diseases / Q000473:pathology; D017510:Protein Folding
chemical_list: D000682:Amyloid; D010455:Peptides