Numerous experimental studies have suggested that polypeptide chains of large amyloidogenic regions zig-zag in xcexb2-serpentine arrangements. These xcexb2-serpentines are stacked axially and form the superpleated xcexb2-structure. Despite this progress in the understanding of amyloid folds, the determination of their 3D structure at the atomic level is still a problem due to the polymorphism of these fibrils and incompleteness of experimental structural data. Today, the way to get insight into the atomic structure of amyloids is a combination of experimental studies with bioinformatics.