title: FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.
abstract: The presence of beta-sheets in the core of amyloid fibrils raised questions as to whether or not beta-sheet-containing proteins, such as transthyretin, are predisposed to form such fibrils. However, we show here that the molecular structure of amyloid fibrils differs more generally from the beta-sheets in native proteins. This difference is evident from the amide I region of the infrared spectrum and relates to the distribution of the phi/psi dihedral angles within the Ramachandran plot, the average number of strands per sheet, and possibly, the beta-sheet twist. These data imply that amyloid fibril formation from native beta-sheet proteins can involve a substantial structural reorganization.
authors.affiliation: Institut für Molekulare Biotechnologie (IMB), D-07745 Jena, Germany.
authors.forename: Giorgia
authors.initials: G
authors.lastname: Zandomeneghi
authors.forename: Mark R H
authors.initials: MR
authors.lastname: Krebs
authors.forename: Margaret G
authors.initials: MG
authors.lastname: McCammon
authors.forename: Marcus
authors.initials: M
authors.lastname: Fändrich
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D006801:Humans; D011228:Prealbumin / Q000737:chemistry; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000682:Amyloid; D011228:Prealbumin