Intrinsically Disordered Proteins

Intrinsically Disordered Proteins Latest News

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.

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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 supports protein folding and quality control, and assembles 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.

Source: TH