{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Liu ZH"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["Over a third of residues in the canonical human proteome are predicted to fall within intrinsically disordered protein regions (IDRs), which do not adopt stable folded structures. These IDRs play critical roles in biological regulation and organization, including as targets for post-translational modifications, scaffolds and mediators of biomolecular condensates. To address the pressing need for valid structural models providing biological relevance and enabling functional insight, we developed the AlphaFlex workflow, using IDPConformerGenerator or IDPForge to calculate fully atomistic conformer ensembles for proteins predicted to have disordered regions, modeled in the context of highly confident folded domains from AlphaFold2. We illustrate our approach by generating conformational ensem"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.11.24.690279"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12697672"],"repository":["biostudies-literature"],"pubmed_title":["AlphaFlex: Ensembles of the human proteome representing disordered regions."],"pmcid":["PMC12697672"],"funding_grant_id":["R01 GM127627","R01 GM147677"],"pubmed_authors":["Attafi OA","Ghafouri H","Moses AM","Fawzi NL","Zhang O","Tosatto SCE","De Castro S","Liu ZH","Forman-Kay JD","Monzon AM","Head-Gordon T","Sun K"],"additional_accession":[]},"is_claimable":false,"name":"AlphaFlex: Ensembles of the human proteome representing disordered regions.","description":"Over a third of residues in the canonical human proteome are predicted to fall within intrinsically disordered protein regions (IDRs), which do not adopt stable folded structures. These IDRs play critical roles in biological regulation and organization, including as targets for post-translational modifications, scaffolds and mediators of biomolecular condensates. To address the pressing need for valid structural models providing biological relevance and enabling functional insight, we developed the AlphaFlex workflow, using IDPConformerGenerator or IDPForge to calculate fully atomistic conformer ensembles for proteins predicted to have disordered regions, modeled in the context of highly confident folded domains from AlphaFold2. We illustrate our approach by generating conformational ensem","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-30T03:30:18.018Z","creation":"2026-06-30T03:23:08.377Z"},"accession":"S-EPMC12697672","cross_references":{"pubmed":["41394673"],"doi":["10.1101/2025.11.24.690279"]}}