title: Ideas of order for amyloid fibril structure.
abstract: Although we know a significant amount about amyloid structure from low-resolution methods, the nature of the fundamental amyloid fibril folding motif remains unknown. Recent data are keeping one model, based on the parallel beta helix, in the foreground of speculation on the molecular make-up of amyloid.
authors.affiliation: Graduate School of Medicine, University of Tennessee Medical Center, Knoxville, TN 37920, USA. rwetzel@mc.utmck.edu
authors.forename: Ronald
authors.initials: R
authors.lastname: Wetzel
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D017772:Amyloid Neuropathies / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000682:Amyloid