Fig. 2

Physico-chemical determinants of protein insolubility. Comparing low-solubility (LS) and high-solubility (HS) proteins in three eukaryotic cells [15], we found that a LS proteins are structurally disordered in human and mouse (red dots indicate enrichments in LS proteins).b The Boxplotter algorithm indicates that there is a significant difference between aggregation-propensities of HS and LS groups in yeast (p-value = 10⁻¹¹; Mann–Whitney–Wilcoxon test; area under the ROC curve = 0.72), which is c inversely related to protein abundance (p-value = 10⁻⁹; Mann–Whitney–Wilcoxon test; area under the ROC curve = 0.70), in agreement with previous evolutionary observations [30–32]. In all organisms, we find d more nucleic acid binding in LS fractions. e, f LS proteins are enriched in nucleic-acid binding ability (Additional file 1: Figure S1), as shown with cleverGO analysis on human and yeast. The links to multiCM, Boxplotter and cleverGO analyses are available at http://www.tartaglialab.com/cs_multi/confirm/737/6065feed14/