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We developed a predictor of protein solubility based on the physico-chemical properties of amino acid sequences. We found that disorder, coil and hydrophilicity propensities best discriminate between soluble and insoluble proteins. Polar residues are associated with high coil and disorder propensities P, E, S, K and Q are the most disorder-prone residues and N, D, G, H and P are the most coil-prone ones.

a tool to predict the solubility of individual proteins based on physicochemical properties

ccSol omics
a method to study protein solubility in large datasets using mutational analysis and E. coli expression

To run the software locally, you should agree to the terms of the Academic License Agreement, which can be found here.