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Intrinsically Disordered Proteins02:18

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Exploring Protein Intrinsic Disorder with MobiDB.

Alexander Miguel Monzon1, András Hatos1, Marco Necci1

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

Methods in Molecular Biology (Clifton, N.J.)
|July 23, 2020
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins lack fixed structures. MobiDB is a key resource for protein disorder and mobility data, offering predictions and curated annotations via an accessible web server.

Keywords:
DatabaseDisorder annotationDisorder predictionIDPIDRIntrinsic disorderIntrinsically disordered proteinsIntrinsically disordered regionsMobiDBStructural flexibility

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Many proteins lack fixed 3D structures under physiological conditions, a state known as intrinsic disorder.
  • Understanding protein disorder is crucial for comprehending biological function and disease mechanisms.

Purpose of the Study:

  • To describe the data available in MobiDB, a comprehensive repository for protein disorder and mobility annotations.
  • To guide users on accessing and utilizing intrinsic disorder information from MobiDB.

Main Methods:

  • MobiDB integrates curated annotations from various databases.
  • It incorporates indirect disorder evidence derived from structural data.
  • Disorder predictions are generated directly from protein sequences.

Main Results:

  • MobiDB provides an exhaustive overview of intrinsic protein disorder.
  • The resource combines multiple data sources for comprehensive annotation.
  • A user-friendly web server facilitates visualization and exploration of disorder data.

Conclusions:

  • MobiDB serves as a central hub for intrinsic disorder and protein mobility data.
  • The repository enhances the study of disordered proteins through integrated data and accessible tools.
  • Researchers can effectively leverage MobiDB for detailed analysis of protein structural flexibility.