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We analyzed the pH-induced mobility changes in moPrP C α-helix and β-sheets by cysteine-scanning site-directed spin labeling (SDSL) with ESR. Nine amino acid residues of α-helix1 (H1, codon 143–151), four amino acid residues of β-sheet1 (S1, codon 127–130), and four amino acid residues of β-sheet2 (S2, codon 160–163) were substituted for by cysteine residues. These recombinant mouse PrP ...
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