Ontology highlight
ABSTRACT:
SUBMITTER: White HE
PROVIDER: S-EPMC2726924 | biostudies-literature | 2009 May
REPOSITORIES: biostudies-literature
Journal of molecular biology 20090405 1
Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is known about the assembly contacts that define the fibril architecture. Here we present a set of three-dim ...[more]