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.

SUBMITTER: Zandomeneghi G 

PROVIDER: S-EPMC2287307 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature