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_3
Snippet: In this study, we investigated the experimental outcomes of 12,216 recombinant proteins expressed in Escherichia coli from the 'Protein Structure Initiative:Biology' (PSI:Biology) (Chen et al. 2004; Acton et al. 2005) . We showed that protein structural flexibility is more accurate than other protein sequence properties in predicting solubility (Craveur et al. 2015; M. Vihinen, Torkkila, and Riikonen 1994) . Flexibility is a standard feature that.....
Document: In this study, we investigated the experimental outcomes of 12,216 recombinant proteins expressed in Escherichia coli from the 'Protein Structure Initiative:Biology' (PSI:Biology) (Chen et al. 2004; Acton et al. 2005) . We showed that protein structural flexibility is more accurate than other protein sequence properties in predicting solubility (Craveur et al. 2015; M. Vihinen, Torkkila, and Riikonen 1994) . Flexibility is a standard feature that appears to have been overlooked in previous solubility prediction attempts. On this basis, we derived a set of 20 values for the standard amino acid residues and used them to predict solubility. We call this new predictor the 'Solubility-Weighted Index' (SWI). SWI is a powerful predictor of solubility, and a good proxy for global structural flexibility. In addition, SWI outperforms many existing de novo protein solubility prediction tools.
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