Fig. 5: A putative α-helix in the P17 tag was not required for solubility enhancement. | Nature Communications

Fig. 5: A putative α-helix in the P17 tag was not required for solubility enhancement.

From: A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments

Fig. 5

a Amino acid sequences of wild-type (wt) P17 tag (P17-WT) and it's mutant (P17-A25P) with alanine 25 substituted by proline. The predicted α-helix formed by P17 tag residues 22–29 is depicted as a cylinder. Proline 25 of P17-A25P mutant is shown in red. b Representative western blot to determine the solubility of MA18/7-scFv-HA protein and its two derivatives with C-terminally fused P17-WT and P17-A25P tags. T total protein, S soluble protein. c Solubility of MA18/7-scFv-HA protein and its derivatives determined by three independent experiments. d Fold change of solubility of MA18/7-scFv-HA-P17 and MA18/7-scFv-HA-P17-A25P proteins compared to MA18/7-scFv-HA protein. Data are presented as mean values ± SD. The statistical significance of differences between the two experimental groups was assessed by one-way ANOVA.

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