Fig. 2: Consensus toxin expression, purification, and secondary structure analysis. | Communications Chemistry

Fig. 2: Consensus toxin expression, purification, and secondary structure analysis.

From: Structural mechanisms behind the neutralisation of long-chain α-neurotoxins by broadly neutralising VHHs discovered using a consensus antigen

Fig. 2

A Schematic representation of the vector employed for electroporation of LCC into K. phaffii. LCC, in phase with the AOX1 promoter, is preceded by the α-mating factor secretion signal (α-MF) and an 6xHis-tag (His). B SDS-PAGE analysis of the supernatant samples collected at 24 h, 48 h, 72 h, and 96 h during the expression as well as the flow-through (FT), wash (W), and elution (E) fractions collected during the affinity purification. C Circular dichroism spectra comparing the secondary structure of LCC (pink) to a native long-chain α-neurotoxin: α-cobratoxin from N. kaouthia (black).

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