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Protein Sci. 2004 Dec;13(12):3314-21. Epub 2004 Nov 10.

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

Author information

1
Institut für Molekulare Biotechnologie (IMB), D-07745 Jena, Germany.

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.

PMID:
15537750
PMCID:
PMC2287307
DOI:
10.1110/ps.041024904
[Indexed for MEDLINE]
Free PMC Article

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