Protein Mutation Modeling and G6PD Screening
Two linked computational workstreams: multimodal mutation analysis over sequence and structure, followed by a focused study of how the R166H variant changes G6PD structure and small-molecule binding profiles.
This page reports the maturity and evidence documented in Ethosoft's working archive. It does not imply peer review, regulatory clearance, or clinical validation.
Methods and evidence
Protein Mutation Modeling and G6PD Screening
Two linked computational workstreams: multimodal mutation analysis over sequence and structure, followed by a focused study of how the R166H variant changes G6PD structure and small-molecule binding profiles.
- Mutation models
- NCBI cDNA and protein data, AlphaFold structures, a GNN, sequence-based XGBoost/ensemble models, and a combined multimodal model. The brief reports F1 scores of 72%, 84%, and 94% respectively.
- G6PD case study
- Wild-type and R166H G6PD sequences modeled with AlphaFold and compared at the structural level.
- Screen
- More than 8,000 DrugCentral compounds were filtered with RDKit; 3,799 molecules were docked against both forms with GNINA.
- Analysis
- Binding energies, mutant-versus-wild-type ΔΔG, CNN pose scores, distributions, and top-ligand comparisons.
Evidence boundary: the F1 values are project-reported and the docking results are computational hypotheses. Neither establishes a therapy or proves restoration of protein function without independent and laboratory validation.