(GIST OF SCIENCE REPORTER) Intrinsically Disordered Proteins

(JANUARY-2026)

Intrinsically Disordered Proteins

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.