Unknown

Dataset Information

0

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

altmetric image

Publications

FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.

Zandomeneghi Giorgia G   Krebs Mark R H MR   McCammon Margaret G MG   Fändrich Marcus M  

Protein science : a publication of the Protein Society 20041110 12


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 ave  ...[more]

Similar Datasets

| S-EPMC3311365 | biostudies-literature
| S-EPMC7553346 | biostudies-literature
| S-EPMC4472244 | biostudies-literature
| S-EPMC2910621 | biostudies-literature
| S-EPMC7335782 | biostudies-literature
| S-EPMC5618150 | biostudies-literature
| S-EPMC2587602 | biostudies-literature
| S-EPMC2427364 | biostudies-literature
| S-EPMC4648968 | biostudies-literature
| S-EPMC2922021 | biostudies-literature