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#protein folding Open access Sep 2026

Inverse FoldDir: Structure-conditioned Protein Sequence Design by Dirichlet Flow Matching

Inverse FoldDir is a structure-conditioned protein redesign method that combines structural recovery, user control, experimental validation, and a natural route toward future property-guided sampling that performs iterative denoising on the amino acid probability simplex.

Alp Tartici, M. Stojkovic, An-Ru Tian et al. · 0 citations
Open access Aug 2026

Homology-Based Variant-Effect Predictors Break Down on Cytochrome P450 Pharmacogenes

Drawing on evidence that a variant’s effect can depend on the drug, it is hypothesized that substrate identity is the key missing feature in current models, and that predicting function for these multi-substrate enzymes may require redefining function as substrate-conditioned.

Helen Z. Xu, I. Samori, Gowri Nayar et al. · 0 citations

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