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Intrinsically Disordered Proteins

Jan. 17, 2026

Researchers have developed a deep-learning tool named Disobind that can predict how Intrinsically Disordered Proteins (IDP) latch on to their binding partners

About Intrinsically Disordered Proteins:

  • Intrinsically disordered proteins are defined as proteins or regions of proteins that lack a fixed or ordered three-dimensional structure under biological conditions.
  • Other Names: Also called natively unfolded or intrinsically unstructured proteins.
  • These are important for cellular signaling and regulation.
  • Functions of Intrinsically Disordered Proteins:
    • They are shape shifting molecules vital to cellular communication.
    • They don’t form a fixed structure.
    • They guide signalling networks.
    • They help proteins move and find partners within the cell, regulate which genes are switched on or off,
    • IDP support protein folding and quality control, and assemble flexible cellular hubs called condensates.

Key Facts about Disobind Tool

  • It is developed by the researchers of National Centre for Biological Sciences (NCBS), Tata Institute of Fundamental Research, Bengaluru.
  • Features of Disobind Tool
    • It is open-source and freely available for researchers worldwide.
    • It analyses the protein sequences and uses protein language models (a form of AI trained on millions of known protein sequences).
    • No structural info needed: It does not require any structural information or sequence alignments, making it super convenient.
    • High accuracy: Disobind outperformed popular tools like AlphaFold-multimer and AlphaFold3 in tests on new protein pairs.
    • Disobind delivered consistently higher accuracy when tested on new protein pairs it had not seen before.
    • Applications of the tool could span from disease biology to drug design.

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