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Fig. 1 | BMC Research Notes

Fig. 1

From: Effects of a naturally occurring amino acid substitution in bovine PrP: a model for inherited prion disease in a natural host species

Fig. 1

Comparison of wild-type and E211K bovine prion protein properties. a Thermal denaturation of wild-type and E211K bovine recombinant prion proteins. Tm results were consistent across multiple independent recombinant PrP preparations. Data points represent the results of a representative experiment (mean thermodynamic parameters for each mutant ± standard deviation, across 4–7 replicate curves, are provided in the text). 95% confidence intervals for the Tm were 68.3–68.7 °C (wild-type) and 65.6–65.9 °C (E211K). b GdnHCl denaturation of wild-type and E211K bovine recombinant prion proteins at 23 °C. A reduction in signal was noted between 0 and 0.6 M GdnHCl, which we propose is due to disruption of aggregative interactions, due to the long unstructured N-terminus on this version of the bovine PrPC protein in particular; however, an initial baseline was well-defined between 0.6 and 1.4 M GdnHCl, which was used for the curve fitting. Mean thermodynamic parameters ± standard deviation are provided in the text for each protein

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