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Biochemistry. 1991 Aug 6;30(31):7672-80.

Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy.

Author information

1
NIAID, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840.

Erratum in

  • Biochemistry 1991 Oct 29;30(43):10600.

Abstract

A protease-resistant form of the protein PrP (PrP-res) accumulates in tissues of mammals infected with scrapie, Creutzfeldt-Jakob disease, and related transmissible neurodegenerative diseases. This abnormal form of PrP can aggregate into insoluble amyloid-like fibrils and plaques and has been identified as the major component of brain fractions enriched for scrapie infectivity. Using a recently developed technique in Fourier transform infrared spectroscopy which allows protein conformational analysis in aqueous media, we have studied the secondary structure of the proteinase K resistant core of PrP-res (PrP-res 27-30) as it exists in highly infectious fibril preparations. Second-derivative analysis of the infrared spectra has enabled us to quantitate the relative amounts of different secondary structures in the PrP-res aggregates. The analysis indicated that PrP-res 27-30 is predominantly composed of beta-sheet (47%), which is consistent with its amyloid-like properties. In addition, significant amounts of turn (31%) and alpha-helix (17%) were identified, indicating that amyloid-like fibrils need not be exclusively beta-sheet. The infrared-based secondary structure compositions were then used as constraints to improve the theoretical localization of the secondary structures within PrP-res 27-30.

PMID:
1678278
DOI:
10.1021/bi00245a003
[Indexed for MEDLINE]

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