Author: Bikash K. Bhandari; Paul P. Gardner; Chun Shen Lim
Title: Solubility-Weighted Index: fast and accurate prediction of protein solubility Document date: 2020_2_16
ID: 2rpr7aph_14
Snippet: To understand the properties of soluble and insoluble proteins, we determined the enrichment of amino acid residues in the PSI:Biology targets relative to the eSOL sequences (see Methods). We observed that the PSI:Biology targets are enriched in charged residues lysine (K), glutamate (E) and aspartate (D), and depleted in aromatic residues tryptophan (W), albeit to a lesser extend for insoluble proteins (Supplementary Fig S7A) . As expected, cyst.....
Document: To understand the properties of soluble and insoluble proteins, we determined the enrichment of amino acid residues in the PSI:Biology targets relative to the eSOL sequences (see Methods). We observed that the PSI:Biology targets are enriched in charged residues lysine (K), glutamate (E) and aspartate (D), and depleted in aromatic residues tryptophan (W), albeit to a lesser extend for insoluble proteins (Supplementary Fig S7A) . As expected, cysteine residues (C) are enriched in the PSI:Biology insoluble proteins, supporting previous findings that cysteine residues contribute to poor solubility in the E. coli expression system (Diaz et al. 2010; Wilkinson and Harrison 1991) .
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