Figure 1.

Effect of mutations on ALK kinase domain stability. All 19 possible mutations along with the synonymous mutations that the residue mutates to itself at each position in ALK kinase domain are colored on a vertical bar in terms of their stability relative to wide-type ALK. The values of ΔΔG_fold are binned into seven categories: highly stabilizing (ΔΔG_fold < −1.84 kcal·mol⁻¹) and highly destabilizing (ΔΔG_fold > 1.84 kcal·mol⁻¹); stabilizing (−1.84 kcal·mol⁻¹ < ΔΔG_fold < −0.92 kcal·mol⁻¹) and destabilizing (0.92 kcal·mol⁻¹ < ΔΔG_fold < 1.84 kcal·mol⁻¹); slightly stabilizing (−0.92 kcal·mol⁻¹ < ΔΔG_foldd < −0.46 kcal·mol⁻¹) and slightly destabilizing (0.92 kcal·mol⁻¹ < ΔΔG_fold < 1.84 kcal·mol⁻¹); and neutral (−0.46 kcal kcal·mol⁻¹ < ΔΔG_fold < 0.46 kcal·mol⁻¹).