Figure 2: Analysis of binding affinity for P-series VH variants with single wild-type reversion mutations. | Scientific Reports

Figure 2: Analysis of binding affinity for P-series VH variants with single wild-type reversion mutations.

From: Efficient affinity maturation of antibody variable domains requires co-selection of compensatory mutations to maintain thermodynamic stability

Figure 2

The equilibrium association constant (KA) values of VH variants containing single reversion mutations were evaluated using yeast surface display and flow cytometry (PBS + 1 g/L BSA). The reversion mutations are highlighted in black (P1), green (P2), blue (P3) and red (P4). The measurements are averages of multiple independent experiments (n = 3–7) and the error bars are standard deviations. A two-tailed Student’s t-test was used to judge statistical significance [p-values < 0.05 (*) or 0.01 (**)]. The statistical significance of P1 and its associated reversion mutants (P11L, K45E, G82bS and R100dG; †) could not be computed because of the low affinity of these variants.

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