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Related Concept Videos

Intrinsically Disordered Proteins02:18

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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DisProt in 2026: enhancing intrinsically disordered proteins accessibility, deposition, and annotation.

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Summary

DisProt, a database for intrinsically disordered proteins (IDPs), has expanded its evidence and features. It now integrates computational predictions and enhances data accessibility for researchers studying protein disorder.

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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) and regions (IDRs) lack stable 3D structures, playing crucial roles in cellular functions.
  • Databases like DisProt are essential for curating and disseminating experimental evidence on IDPs and IDRs.
  • The growing body of research on IDPs necessitates continuous updates and improvements in data management and accessibility.

Purpose of the Study:

  • To present the latest release of the DisProt database, highlighting its growth and new features.
  • To improve the integration and accessibility of experimental data on intrinsically disordered proteins and regions.
  • To enhance the utility of DisProt for researchers through new functionalities and data expansion.

Main Methods:

  • Systematic adoption of Minimum Information About Disorder Experiments (MIADE) guidelines for detailed annotation.
  • Expansion of DisProt data through BLAST-based homology propagation in MobiDB.
  • Integration of computational predictions as valid evidence alongside experimental data.
  • Updates and restructuring of the Intrinsically Disordered Protein (IDP) Ontology.

Main Results:

  • DisProt now contains 3201 IDPs and 13,347 pieces of evidence, with over 1500 new structural state and 1300 new function annotations.
  • MIADE adoption has more than doubled annotations with experimental details, improving interpretability.
  • Disorder regions and interacting peptides have been extended to hundreds of thousands of proteins via homology propagation.
  • The database now integrates computational predictions and features an updated IDP Ontology for enhanced accuracy and interoperability.

Conclusions:

  • The enhanced DisProt database offers a more comprehensive and accessible resource for studying intrinsically disordered proteins.
  • New features, including integrated computational predictions and an updated ontology, improve data accuracy and semantic clarity.
  • DisProt's evolution into a hybrid knowledgebase and deposition system, alongside community engagement tools, supports broader research participation.