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NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences.

Hiroto Anbo1, Hiroki Amagai1, Satoshi Fukuchi1

  • 1Department of Life Science and Informatics, Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan.

Biophysics and Physicobiology
|December 11, 2020
PubMed
Summary

We developed NeProc, a new program to predict disordered binding regions in intrinsically disordered proteins. This tool overcomes data limitations by using structural domain and intrinsically disordered region data, not binding region data.

Keywords:
binding regionsintrinsically disordered proteinneural networkstructure prediction

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Area of Science:

  • Proteomics
  • Bioinformatics
  • Computational Biology

Background:

  • Intrinsically disordered proteins (IDPs) feature functional segments in disordered regions crucial for molecular interactions and regulatory roles.
  • Existing databases for these disordered binding regions are limited, hindering further research and development.
  • Predicting these regions without direct binding data is essential for advancing IDP studies.

Purpose of the Study:

  • To develop a novel computational tool, NeProc, for predicting disordered binding regions in intrinsically disordered proteins.
  • To overcome the scarcity of experimental data on disordered binding regions by utilizing alternative data sources.
  • To provide a reliable method for identifying functional segments within IDPs.

Main Methods:

  • Developed NeProc, a program that predicts disordered binding regions using only structural domain and intrinsically disordered region data.
  • Input sequences are converted into position-specific score matrices.
  • Employed two neural networks with different window sizes (short and long) for enhanced prediction accuracy.

Main Results:

  • NeProc demonstrated performance comparable to existing programs for disordered binding region prediction.
  • The program successfully predicted disordered binding regions without relying on direct binding data.
  • This approach effectively addresses the limitations posed by scarce disordered binding region datasets.

Conclusions:

  • NeProc offers a viable solution to the challenge of limited data for disordered binding region prediction.
  • The tool's success highlights the potential of using structural and disorder information for predicting functional protein segments.
  • NeProc can aid in the discovery and characterization of functionally important regions in intrinsically disordered proteins.