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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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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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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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MOBIDB in 2025: integrating ensemble properties and function annotations for intrinsically disordered proteins.

Damiano Piovesan1, Alessio Del Conte1, Mahta Mehdiabadi1

  • 1Department of Biomedical Sciences, University of Padova, Padua 35131, Italy.

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Summary

MobiDB now offers enhanced protein disorder information with faster predictions and improved data access. This update provides deeper insights into intrinsic disorder functions and structural details for researchers.

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Area of Science:

  • Bioinformatics
  • Structural Biology
  • Computational Biology

Background:

  • Intrinsic protein disorder is crucial for cellular functions.
  • Existing databases require updates for comprehensive disorder information.
  • MobiDB aggregates structural and functional data on protein disorder.

Purpose of the Study:

  • To detail recent improvements in the MobiDB database.
  • To enhance data accessibility, capture, and documentation.
  • To provide novel functional knowledge about intrinsic disorder.

Main Methods:

  • Updated all underlying pipeline modules for data processing.
  • Enhanced prediction module for speed and structural detail (extended/compact).
  • Improved PDB component to process large cryo-EM structures.
  • Restyled entry pages and reimplemented graphical modules.
  • Standardized annotation provenance using ECO terms.
  • Propagated disorder function from DisProt using sequence similarity and embeddings.

Main Results:

  • Prediction module is ten times faster, distinguishing extended/compact disordered regions.
  • Increased number of processed PDB entries due to enhanced cryo-EM structure processing.
  • Improved user interface with restyled pages and faster graphical rendering.
  • Optimized server for efficient bulk downloads.
  • Standardized annotation provenance and enriched disorder function data.

Conclusions:

  • MobiDB offers a more intuitive interface and expanded functional knowledge of intrinsic disorder.
  • The updated resource facilitates deeper structural and functional analysis of disordered proteins.
  • Enhanced data processing and accessibility benefit the broader research community.