Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L).
Solid State Nucl Magn Reson
; 29(1-3): 183-90, 2006 Feb.
Article
en En
| MEDLINE
| ID: mdl-16256316
ABSTRACT
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 PrP(89-143)(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 (13)C=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 beta-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.
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Bases de datos:
MEDLINE
Asunto principal:
Priones
/
Resonancia Magnética Nuclear Biomolecular
/
Cristalografía
/
Amiloide
Límite:
Animals
Idioma:
En
Revista:
Solid State Nucl Magn Reson
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos