Cambridge University – mv245@cam.ac.uk

Sequence-based prediction of protein solubility

As increasing evidence indicates that the sequences of proteins encode not just their folding but also their solubility and aggregation [1,2], there is great interest in identifying the amino acid code responsible for the maintenance of solubility. We have been developing computational methods to predict different aspects of the aggregation process, including the rates of growth of the aggregates and the regions that promote aggregation [3-6]. In this context, I will review our current understanding and ability to control protein solubility on the basis of the physico-chemical properties of the amino acids.

[1] Chiti et al Nature 424, 805-808 (2003).

[2] Vendruscolo et al. Cold Spring Harb. Perspect. Biol. 3, a010454 (2011).

[3] DuBay et al J. Mol. Biol. 341, 1317-1326 (2004).

[4] Pawar et al J. Mol. Biol. 350, 379-392 (2005).

[5] Tartaglia et al. J. Mol. Biol. 380, 425-436 (2008).

[6] Agostini et al. J. Mol. Biol. 421, 237-241 (2012).

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