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Identification of the interaction sites on bPrP for R12. ( A ) The amino acid sequences of a series of peptide fragments of bPrP. ( B ) The plot of the relative binding of R12 with a series of <t>12-mer</t> peptides covering bPrP 25–131. Amino acid positions 60–88 of bPrP is composed of the four repeats of peptides 10 and 11 (octapeptide repeat region).
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Identification of the interaction sites on bPrP for R12. ( A ) The amino acid sequences of a series of peptide fragments of bPrP. ( B ) The plot of the relative binding of R12 with a series of <t>12-mer</t> peptides covering bPrP 25–131. Amino acid positions 60–88 of bPrP is composed of the four repeats of peptides 10 and 11 (octapeptide repeat region).
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Identification of the interaction sites on bPrP for R12. ( A ) The amino acid sequences of a series of peptide fragments of bPrP. ( B ) The plot of the relative binding of R12 with a series of 12-mer peptides covering bPrP 25–131. Amino acid positions 60–88 of bPrP is composed of the four repeats of peptides 10 and 11 (octapeptide repeat region).

Journal: Nucleic Acids Research

Article Title: Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein

doi: 10.1093/nar/gkp647

Figure Lengend Snippet: Identification of the interaction sites on bPrP for R12. ( A ) The amino acid sequences of a series of peptide fragments of bPrP. ( B ) The plot of the relative binding of R12 with a series of 12-mer peptides covering bPrP 25–131. Amino acid positions 60–88 of bPrP is composed of the four repeats of peptides 10 and 11 (octapeptide repeat region).

Article Snippet: The 12-mer peptide libraries covering bPrP 25–131 were overlapped with a +4 position shift between consecutive peptides (PEP screen, Sigma-Aldrich).

Techniques: Binding Assay