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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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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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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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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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

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QSProteome: A Community-Driven Interactive Platform for Large-Scale Exploration and Evaluation of Predicted Protein

Edward A Catoiu, Delina Kambo, Brianna Rodriguez

    Biorxiv : the Preprint Server for Biology
    |September 26, 2025
    PubMed
    Summary

    QSProteome is a new platform for modeling and refining protein structures. This community-driven resource makes proteome-scale structural biology data accessible and promotes collaborative refinement of protein complexes.

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    Area of Science:

    • Structural biology
    • Computational biology
    • Bioinformatics

    Background:

    • Quaternary protein structure modeling and evaluation are crucial for understanding biological functions.
    • Existing resources often lack comprehensive, community-driven refinement capabilities for large-scale protein complex data.

    Purpose of the Study:

    • To introduce QSProteome, a community-scale platform for modeling, evaluating, and refining quaternary protein structure.
    • To provide a dynamic, scalable infrastructure for proteome-scale structural biology research.
    • To enable community-led assessment and iterative refinement of protein complex structures.

    Main Methods:

    • Hosting 35,528 unique modeled protein assemblies from BioCyc and ComplexPortal databases.
    • Utilizing interactive 3D visualization, confidence metrics, structural alignments, and functional annotations for each model.
    • Implementing a cloud-based server for continuous user uploads and automated processing, including a gamified re-curation workflow.

    Main Results:

    • QSProteome currently hosts over 35,528 modeled protein assemblies, covering extensive curated complex databases.
    • The platform successfully processed and validated over 54,000 models within 14 weeks.
    • A community-led assessment of 1,547 ABC transporter complexes was facilitated through the re-curation workflow.

    Conclusions:

    • QSProteome provides a unified, searchable, and extensible framework for proteome-scale structural biology.
    • The platform enhances accessibility and reusability of structural data, fostering discovery and annotation.
    • Community engagement through gamified workflows drives iterative refinement and advances collaborative structural biology research.