Part:BBa_K3468088:Experience

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Applications of BBa_K3468088

We builded a model of the mutant (A202C-E231c), using Pymol for visual inspection (geometric criteria, see Figure 4 and Table 1), and finally using FoldX for evaluation. During visual inspection in Pymol, we found that this disulfide bond is far from the catalytic triad, far from the inside of the protein, and met the disulfide bond geometry criteria. DDG is -2.454kcal/mol evaluated by FoldX.

Fig.2 Overview of A202C and E231C

Fig.3 Structure feature of A202C and E231C

Fig.4 Disulfide bond with the geometric parameters that were used as selection criteria in their computational design.

Table1. Geometric criteria for computational design of disulfide bonds.

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