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. 2007 Apr 12;8:6. doi: 10.1186/1471-2091-8-6

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Copyright © 2007 Rigter et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Overview of PrP^Csecondary structures and antibody epitopes versus peptide-array binding pattern and Kyte-Doolittle hydrophilicity plot. Schematic representation of PrP^Cshowing signal sequences, β-sheets (S1, S2), α-helices (H1, H2, H3), disulfide bridge site (S-S), glycosylation sites (CHO) and relative positions of the antibodies used in this study. The sequence of PrP is lined up with both the Kyte-Doolittle hydrophilicity plot (negative = hydrophobic and positive = hydrophilic) and the relative binding pattern found with the ovine peptide-array.