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# Intrinsically Disordered Proteins

2 related articles

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  1. bioRxiv

    bAIes drops its AlphaFold2-only constraint: six structure predictors yield comparable atomic-resolution ensembles of disordered proteins

    bAIes originally drew structural information only from AlphaFold2 distograms to build atomic-resolution conformational ensembles of intrinsically disordered proteins. It now accepts six predictors, AlphaFold2, AlphaFold3, Boltz-1, Boltz-2, ESMFold and ESMFold2, and was compared on NMR and SAXS data for 17 disordered proteins. Ensembles from every predictor reach average accuracy comparable to the original AlphaFold2 version, best on local observables such as chemical shifts, RDCs and 3J couplings, and weaker on long-range and global observables such as PREs and SAXS.

    Institut Pasteur
    Vincent Schnapka（First author）Massimiliano Bonomi（Corresponding author）
    bAIesIntrinsically Disordered ProteinsProtein Structure PredictionMolecular Dynamics
  2. Nature Communications

    Disordered proteins get all-atom ensembles in one diffusion pass, matching NMR and SAXS without reweighting

    IDPForge repurposes ESMFold's attention and structure modules as a diffusion generator that produces all-atom ensembles of intrinsically disordered proteins and regions directly from sequence, without per-sequence training, coarse-grained back-mapping or ensemble reweighting. On 32 test sequences with NMR and/or SAXS data it reaches a normalized total X-EISD score of 0.89, against 0.57 for IDPConformerGenerator, 0.58 for IDPFold and 0.58 for CALVADOS, and it can denoise only the disordered region around a folded template.

    University of California, BerkeleyUniversity of TorontoHospital for Sick Children
    Oufan Zhang（First author）Stefano De Castro（First author）Teresa Head‐Gordon（Corresponding author）
    IDPForgeDiffusion ModelIntrinsically Disordered ProteinsProtein Structure Prediction

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