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. 2019 Feb 28;9:3123. doi: 10.1038/s41598-019-39781-3

Figure 11.

Figure 11

Comparison of the sequences of 6aJL2 protein predicted to be fibrillogenic/aggregation-prone by the computational tools ZipperDB26 and AmylPred228 and the fibril-forming segments identified by the two different experimental strategies implemented in this study. Strategy 1 and 2 refer to the “prediction-based” and “proteolysis-based” strategies, respectively, which are described in detail in Methods. The segments of the protein folded as β-strand and α helix are represented as red arrows and green cylinders, respectively. The Framework (FR) and Complementarity Determining Regions (CDR) are indicated at the top of the figure. The sequence of protein 6aJL2 is shown in “one letter” code. The conserved intradomain disulphide bond Cys23-Cys88 is shown as a dashed line in the sequence of 6aJL2 protein and in the tryptic fragment Thr18-Arg25-S-S-Thr80-Lys103. The black curly bracket below the sequence SSGSIASNYVQWYQQR indicates the segment that proved to be sensitive to Pro mutation by scanning proline mutagenesis analysis.