Back to search

Article

Decoding conformational heterogeneity across disordered proteomes

2026-03-16

Abstract excerpt

Intrinsically disordered proteins (IDPs) comprise nearly one-third of the human proteome and play key roles in regulation, signaling, and disease, yet their dynamic nature has resisted accurate structural prediction even by the state of the art deep-learning methods. Here we introduce AI-IDP, a framework combining established deep-learning structure prediction of isolated short IDP fragments with their flexible ph...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
93b3ce5c-3015-5e55-9993-0b0e0b979036
DOI
10.64898/2026.03.13.711260
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Decoding conformational heterogeneity across disordered proteomesDOI 10.64898/2026.03.13.711260
Select a neighboring publication to make it the new centre.