AlphaFlex: Ensembles of the human proteome representing disordered regions.

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

SUBMITTER: Liu ZH 

PROVIDER: S-EPMC12697672 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature