title: Structural aspects of amyloid formation.
abstract: Amyloid fibrils are highly organized and generally insoluble protein aggregates rich in β secondary structure that can be formed by a wide range of sequences. They have been the object of intense scrutiny because their formation has been associated with a number of neurodegenerative disorders such as Alzheimer's, Parkinson's, Huntington's, and Creutzfeldt-Jakob's diseases. As a consequence of these efforts, much is now known about the properties of proteins that render them prone to form amyloid fibrils, about the mechanism of fibrillation, about the molecular structures of the fibrils, and about the forces that stabilize them. The relationship between the structural properties of the monomeric protein and those of the corresponding aggregate has been, in particular, intensively studied. In this chapter, we will provide an account of current knowledge on this intriguing relationship and provide the reader with key references about this topic.
authors.affiliation: ICREA, Barcelona, Spain.
authors.forename: Xavier
authors.initials: X
authors.lastname: Salvatella
mesh_terms: D000682:Amyloid / Q000096:biosynthesis* / Q000737:chemistry*; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013997:Time Factors
chemical_list: D000682:Amyloid