Abstract
A key event in the pathogenesis of prion diseases is the change in structure of the normal cellular form of the prion protein from a predominantly α-helix form to the β-sheet-rich prion protein found in disease-associated tissue. To allow more detailed structural research into PrP misfolding, it is necessary to have techniques which enable enrichment of the β-sheet content in recombinant PrP.
This method describes the procedure for inducing β-folding of recombinant PrP to resemble a disease-associated structure and ultimately produce soluble β-folded recombinant PrP.
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Ellett, L.J. (2017). Method for Folding of Recombinant Prion Protein to Soluble β-Sheet Secondary Structure. 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_2
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DOI: https://doi.org/10.1007/978-1-4939-7244-9_2
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