Figure 3 | Scientific Reports

Figure 3

From: A high-performance thioredoxin-based scaffold for peptide immunogen construction: proof-of-concept testing with a human papillomavirus epitope

Figure 3

Circular dichroism analysis of empty and L2 tripeptide containing EcTrx and PfTrx.

(a) Far-UV CD spectra (recorded at 25°C) of the empty (solid line) and the L2 insert-containing (dotted line) EcTrx protein (10 μM in PBS) purified by metal-affinity chromatography. (b) Same as (a) for PfTrx. Spectra are given as molar ellipticity [θ] values at different wavelengths (λ). Secondary structure alterations produced by the incorporation of the L2(20-38)3 tripeptide are apparent. (c) Far-UV CD analysis of metal affinity-purified EcTrx-L2(20-38)3 (10 μM in PBS). Data are presented as variations of molar ellipticity [θ] at 200 nm upon unfolding (25–85°C; close dots, gray line) and refolding (85–25°C; open dots, black line). Temperature-dependent midpoint transitions at 52.1°C (unfolding) and 49.9°C (refolding) were calculated. (d) Same as in panel C for PfTrx-L2(20-38)3, for which no changes of [θ] at 200 nm were observed.

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