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. 2026 Jul 9;6(5):100507. doi: 10.1016/j.xjidi.2026.100507

Figure 5.

Figure 5

In silico prediction of structural and thermodynamic impacts of MYH9 variants on Myosin-9 dimer stability and binding affinity. AlphaFold-Multimer was used to generate the predicted Myosin-9 dimer structures (chain A and chain B), including the WT and variant forms. (a) Myosin-9 Gly455S-Ile1626V:Arg1497Gln (also G455S-I1626V:R1497Q) sequence variants. WT (teal) and variants (brown) structures showing the interface of interactions for Ile1626 (I1626, top panels), Arg1497 (R1497, middle panels), and Gly455 (G455, bottom) are shown. Residues are shown as sticks and colored on the basis of atom type. (b) The table quantifies the impact of each sequence variant or their combination on key protein characteristics: Variant(s) in Myosin-9: Lists the specific amino acid changes (eg, G455S, R1497Q, I1626V) and indicates which chain (A or B) of the Myosin-9 dimer the sequence variant is located on. Change in protein stability (ΔΔG, kcal/mol): Represents the predicted change in the overall thermodynamic stability of the protein due to the sequence variant (kcal/mol). Positive values typically indicate destabilization, whereas negative values suggest stabilization; change in chain binding affinity (ΔΔG, kcal/mol): Reflects the predicted change in the binding strength between the 2 Myosin-9 dimer chains (A and B) as a result of the mutation; change in residue hydropathy (Δhydropathy): Indicates the predicted change in the hydropathy (hydrophobicity or hydrophilicity) of the mutated residue, with specific values provided. The table includes analyses for single mutations (eg, A: I1626V, A: G455S, B: R1497Q) and combinations, such as the G455S and I1626V mutations on chain A, and their occurrence with R1497Q on chain B, reflecting complex allelic configurations. WT, wild-type.