Stanford team releases FoldDir, a Dirichlet flow-matching model for protein inverse folding
KevinKaichuang · x · 2026-09-16
A Stanford team (Tartici, Jewett, Altman et al.) released FoldDir, a flow-matching, structure-conditioned protein sequence design model for the inverse folding task — finding amino acid sequences compatible with a desired backbone.
The authors report strong computational benchmark results and several functional nanobody redesigns. The preprint, "Inverse FoldDir: Structure-conditioned Protein Sequence Design by Dirichlet Flow Matching," is on bioRxiv.
Related event: Stanford team releases FoldDir for structure-conditioned protein design(2 posts)→
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