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Fig. 13. The experimental k2 values (24) measured at pH 7.5 and 6 for the mutants relative to the wt plastocyanin [ln(k2/k2 WT)] are plotted against the electrostatic potential similarity index, expressed as sqrt(2-2SI) and computed by comparing the wild-type and mutant plastocyanins on the whole proteins (A and B) and on the eastern site (C and D).

Fig. 13. The experimental k2 values (24) measured at pH 7.5 and 6 for the mutants relative to the wt plastocyanin [ln(k2/k2 WT)] are plotted against the electrostatic potential similarity index, expressed as sqrt(2-2SI) and computed by comparing the wild-type and mutant plastocyanins on the whole proteins (A and B) and on the eastern site (C and D).

Site-directed mutagenesis is a valuable techniques for assessing the importance of specific amino acid residues for protein activity. However, the results of these experiments are usually interpreted qualitatively or empirically.

The quantitative approach applied to plastocyanin has been shown to be helpful in providing a physical interpretation of the available experimental data and constitute a promising predictive tool for protein engineering.

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