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Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Protein Organization

Protein Organization

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.
The primary structure of a protein is its amino acid sequence....

Protein-protein Interfaces

Protein-protein Interfaces

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...

Protein-Protein Interfaces

Protein-Protein Interfaces

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Dec 6, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Exploring Manually Curated Annotations of Intrinsically Disordered Proteins with DisProt.

Federica Quaglia¹, András Hatos¹, Damiano Piovesan¹

¹Department of Biomedical Sciences, University of Padova, Padova, Italy.

Current Protocols in Bioinformatics

|October 5, 2020

Summary

This summary is machine-generated.

DisProt is a key resource for intrinsically disordered proteins (IDPs), offering manually curated data. This guide details how to search, access, and interpret IDP annotations for biological research.

Keywords:

DisProt community curation database intrinsically disordered proteins literature curation

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Area of Science:

Biochemistry
Molecular Biology
Bioinformatics

Background:

Intrinsically disordered proteins (IDPs) lack stable tertiary structures but perform vital biological functions.
Research on IDPs has expanded significantly, focusing on their unique properties and roles.
DisProt serves as a primary repository for manually curated IDP data from scientific literature.

Purpose of the Study:

To provide a comprehensive guide on utilizing the DisProt database.
To explain how to explore and interpret manually curated annotations of intrinsically disordered proteins.
To demonstrate practical applications of DisProt through search, programmatic access, and data visualization.

Main Methods:

Literature curation by expert biocurators.
Web interface and REST API for data retrieval and programmatic access.
Case study using the p53 protein to illustrate data interpretation.

Main Results:

DisProt offers up-to-date annotations of intrinsically disordered proteins.
Users can search and download data via the web interface or API.
Detailed protocols are provided for accessing and interpreting DisProt entries, including a p53 example.

Conclusions:

DisProt is an essential resource for researchers studying intrinsically disordered proteins.
The database facilitates the exploration and understanding of IDP functions and characteristics.
The guide empowers the scientific community to effectively use DisProt for their research needs.