Figures
- Mutation of exposed hydrophobic amino acids to arginine to increase protein stability

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Figure 1 Effect of replacement of hydrophobic residues at the surface by arginine on relative production. Ratio of production represents the relative production of each mutant.

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Figure 2 Position of Gly 55 and Leu 57, near Val 14.

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Figure 3 Effect of replacement of hydrophobic residues at the surface by arginine on relative stability. For each mutation, ratio of t50 (t50 mutant/t50 wild type) was calculated for each denaturation agent. * indicates a significant difference with the wild type protein with P

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Figure 4 Position of Phe 225 inside an hydrophobic area at the surface of the protein. (hydrophobic residues have been colored in blue).

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Figure 5 Electrostatic stabilization expected for the charge addition according to the Coulomb's Law (E = q1q2/Dr) with a dielectric constant of 80 by summing the interactions of the new charge with all the other charges of the protein.