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Figure 1.
Figure 1. Primary structure of the human prion protein. The
mature human prion protein consists of residues 23–230. The
amino acid sequence of the OPR region from residues 51 to 91
(gray boxes) is shown at the bottom, where residues
unambiguously assigned in the NMR spectra are underlined. For
the segment 54–89 only a single set of resonance signals was
detected for each repeated amino acid (see the text). Regular
secondary structure elements are represented in black. The
disulfide bond (S–S) between Cys179 and Cys214 is drawn as a
gray line. Arrows at the top indicate N-terminal truncations
sites of the hPrP constructs used in this study.
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