Figure 1: The structural and interaction properties of D. melanogaster TR extensions. | Scientific Reports

Figure 1: The structural and interaction properties of D. melanogaster TR extensions.

From: Computational analysis of translational readthrough proteins in Drosophila and yeast reveals parallels to alternative splicing

Figure 1: The structural and interaction properties of D. melanogaster TR extensions.

The fractions of residues in predicted (a) disordered (by IUPred), (b) low complexity (by SEG), (c) secondary structure (by PSIPRED) and (d) disordered binding regions (by ANCHOR) were calculated for the TR extensions (TRC_E; red) and compared to those for the randomly selected C-termini (RAND_C; yellow) and the C-termini of the TR candidates (TRC_C; grey) using Kruskal-Wallis test coupled with Dunn’s multiple comparison post-hoc test. The p-values indicated above the box plots are adjusted according to the number of comparisons performed in each panel. The significance threshold is further decreased to p = 0.0125 by Bonferroni correction due to the multiplicity of properties compared.

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