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Updated: May 8, 2025
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
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Searching and Using MobiDB Resource 6 to Explore Predictions and Annotations for Intrinsically Disordered Proteins
Maria Cristina Aspromonte1,2, Federica Quaglia1,3,2, Alexander Miguel Monzon4
1Department of Biomedical Sciences, University of Padova, Padova, Italy.
Current Protocols
|December 24, 2024
Summary
MobiDB version 6 offers enhanced knowledgebase of intrinsically disordered proteins (IDPs) and regions (IDRs) with integrated predictions and improved accessibility. This resource aids in understanding protein disorder crucial for cellular functions and diseases.
Area of Science:
- Biochemistry and Molecular Biology
- Bioinformatics and Computational Biology
- Structural Biology
Background:
- Intrinsically disordered proteins (IDPs) constitute ~30% of eukaryotic proteomes and are vital in cellular processes, neurodegenerative disorders, and cancers.
- IDPs' dynamic nature and role in biomolecular condensates present challenges in understanding their function.
- A comprehensive knowledgebase for IDPs and intrinsically disordered regions (IDRs) is essential for scientific research.
Purpose of the Study:
- To introduce MobiDB version 6, a significantly enhanced knowledgebase for intrinsically disordered proteins (IDPs) and regions (IDRs).
- To detail the updated features, including expanded annotation coverage, improved accessibility, and integration of new data sources.
- To provide a protocol for users to effectively utilize MobiDB for disorder prediction, data analysis, and exploration of protein interaction data.
Main Methods:
- Integration of AlphaFoldDB predictions and a new homology transfer pipeline to increase high-quality annotations.
- Updates to the user interface for clearer visualization of disorder, binding, and functional information.
- Development of protocols for searching MobiDB via web interface and REST API, including a case study using the human growth hormone receptor.
Main Results:
- MobiDB version 6 substantially increases the number of entries with high-quality disorder annotations.
- The updated interface provides immediate overviews of protein disorder and function information.
- Protocols demonstrate effective querying, data analysis, and visualization of protein disorder data within MobiDB.
Conclusions:
- MobiDB version 6 represents a major advancement in resources for studying intrinsically disordered proteins and regions.
- The enhanced database and user-friendly protocols facilitate deeper understanding of IDP functions in health and disease.
- MobiDB serves as a critical tool for researchers investigating protein disorder across various scientific domains.
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