We developed a predictor of protein solubility based on the physicochemical 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.
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