1. Tertiary structure characterization with 1H‐NMR at 900 MHz
Tertiary structure characterization with 1H‐NMR at 900 MHz. (A) 1D 1H‐NMR spectrum of recombinant bPrP(23–230).
Tertiary structure characterization with 1H‐NMR at 900 MHz. (A) 1D 1H‐NMR spectrum of recombinant bPrP(23–230). (B) 1D 1H‐NMR spectrum of natural bPrPC. (C,D) Expanded plots of the region 0.9 to −0.1 p.p.m. of the 1H‐NMR spectra of (A) and (B), respectively. In (C), the peaks are labelled with the previously obtained resonance assignments (Lopez Garcia et al, 2000). In (D), a spurious peak is marked with the label X. (E) Location of the methyl groups with high field‐shifted resonance lines in the NMR structure of recombinant bPrP(23–230) (Lopez Garcia et al, 2000). The polypeptide backbone of the C‐terminal domain of bPrP(23–230) is represented by a grey spline function through the α‐carbon positions. The side chains with high field‐shifted methyl 1H‐NMR lines are shown in orange colour, and the aromatic residues that cause the high field shifts of these methyl groups are shown in green. The two N‐glycosylation sites are coloured in cyan. (F,G) Space‐filling models of the C‐terminal globular domain of residues 125–230 on the basis of the NMR structure of recombinant bPrP(23–230). (F) bPrPC with the two glycosylation moieties in blue, the GPI anchor in green and the polypeptide chain in red. (G) bPrPC without the two glycosylation moieties.
Simone Hornemann et al. EMBO Rep. 2004;5:
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