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The α helical content was 29% for 27 kDa 7B2, while the β sheet content was 14%.
The 21 kDa rat and the 27 kDa C. elegans proteins contained even fewer structural elements, with only 18% α helix and 26% β sheet content.
This was first established for prion diseases and the PK resistance was attributed to the amyloid structure with high beta sheet content of the pathological prion protein [ 15].
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This is associated with increasing solubility, stability, and secondary structure β-sheet content of the peptide.
Mutation for diminishing β-sheet content reduced polymerization of cystatin C, thus improving papain-inhibitory activity.
The increased β-sheet content improved film stability under culture conditions.
However, β-sheet content was not affected by degumming time, suggesting that degradation occurred mainly in hydrophilic domains of SF.
The spectrum of the crosslinked sample 3(G) suggests slightly larger β-sheet content than that in the uncrosslinked sample.
The normal, cellular prion protein (PrPC) is converted into PrPSc through a posttranslational process during which it acquires a high β-sheet content.
The beta-sheet content was different at pH2.8 and pH7.2.
PrPSc has a high β-sheet content and prone to aggregation.
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