Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L)

Kwang Hun Lim, Tuan N. Nguyen, Steven M. Damo, Tanya Mazur, Haydn L. Ball, Stanley B. Prusiner, Alexander Pines, David E. Wemmer

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


The peptide fragment 89-143 of the prion protein (carrying a P101L mutation) is biologically active in transgenic mice when in a fibrillar form. Injection of these fibrils into transgenic mice (expressing full length PrP with the P101L mutation) induces a neurodegenerative prion disease (Kaneko et al., J. Mol. Biol. 295 (2000) 997). Here we present solid-state NMR studies of PrP89-143(P101L) fibrils, probing the conformation of residues in the hydrophobic segment 112-124 with chemical shifts. The conformations of glycine residues were analyzed using doubly 13C=O labeled peptides by two-dimensional (2D) double-quantum correlation, and double-quantum filtered dephasing distance measurements. MQ-NMR experiments were carried out to probe the relative alignment of the individual peptides fibrils. These NMR studies indicate that the 112-124 segment adopts an extended β-sheet conformation, though not in a parallel, in register alignment. There is evidence for conformational variability at Gly 113. DQ correlation experiments provide useful information in regions with conformational heterogeneity.

Original languageEnglish (US)
Pages (from-to)183-190
Number of pages8
JournalSolid State Nuclear Magnetic Resonance
Issue number1-3
StatePublished - Feb 2006


  • Alignment
  • Double-quantum NMR
  • Multiple-quantum NMR
  • Prion
  • Solid-state NMR
  • β-helix

ASJC Scopus subject areas

  • Radiation
  • Chemistry(all)
  • Nuclear and High Energy Physics
  • Instrumentation


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