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Solid-State NMR Studies of the Secondary Structure of a Mutant Prion Protein Fragment of 55 Residues That Induces Neurodegeneration
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Solid-State NMR Studies of the Secondary Structure of a Mutant Prion Protein Fragment of 55 Residues That Induces Neurodegeneration
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Journal Article
Solid-State NMR Studies of the Secondary Structure of a Mutant Prion Protein Fragment of 55 Residues That Induces Neurodegeneration
2001
Overview
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in randomly aggregated (dried from water) and fibrillar (precipitated from water/acetonitrile) forms by13C solid-state NMR. Recent studies have shown that the fibrillar form of the P101L mutant of MoPrP(89-143) is capable of inducing prion disease in transgenic mice, whereas unaggregated or randomly aggregated samples do not provoke disease. Through analysis of13C chemical shifts, we have determined that both wild-type and mutant sequence MoPrP(89-143) form a mixture of β-sheet and α-helical conformations in the randomly aggregated state although the β-sheet content in MoPrP(89-143, P101L) is significantly higher than in the wild-type peptide. In a fibrillar state, MoPrP(89-143, P101L) is completely converted into β-sheet, suggesting that the formation of a specific β-sheet structure may be required for the peptide to induce disease. Studies of an analogous peptide from Syrian hamster PrP verify that sequence alterations in residues 101-117 affect the conformation of aggregated forms of the peptides.
Publisher
National Academy of Sciences,National Acad Sciences,The National Academy of Sciences
