FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

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Abstract
The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not β‐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 β‐sheets in native proteins. This difference is evident from the amide I region of the infrared spectrum and relates to the distribution of the ϕ/ψ dihedral angles within the Ramachandran plot, the average number of strands per sheet, and possibly, the β‐sheet twist. These data imply that amyloid fibril formation from native β‐sheet proteins can involve a substantial structural reorganization.