Abstract
According to the protein-only hypothesis of prion propagation, the pathogenesis of prion disease is due to the misfolding of cellular PrP (PrPC) which gives rise to disease-associated PrPSc. This misfolding results in the predominantly α-helix secondary structure of PrP becoming increasingly β-sheet. Prion protein researchers often employ circular dichroism (CD) spectroscopy to rapidly analyze and identify the degree of α-helix and β-sheet content in their recombinant protein and peptide samples. CD is a nondestructive method of determining protein secondary structure and can be used to monitor the protein structural changes in various environments, e.g., pH and temperature. CD can also be used to investigate kinetic and thermodynamic characteristics of proteins and peptides.
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Acknowledgment
This work was supported by National Health and Medical Research Council.
(grant numbers 400202 and 400183) and the Bethlehem Griffiths Research Foundation.
(grant number 802270).
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Ellett, L.J., Johanssen, V.A. (2017). Analysis of Prion Protein Conformation Using Circular Dichroism Spectroscopy. In: Lawson, V. (eds) Prions. Methods in Molecular Biology, vol 1658. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7244-9_3
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DOI: https://doi.org/10.1007/978-1-4939-7244-9_3
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