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Related Concept Videos

Protein-protein Interfaces02:04

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 polypeptide...
Protein Networks02:26

Protein Networks

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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Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Proteomics

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Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
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Mining Proteins with Non-Experimental Annotations Based on an Active Sample Selection Strategy for Predicting Protein

Junzhe Cao1, Wenqi Liu, Jianjun He

  • 1School of Control Science and Engineering, Dalian University of Technology, Dalian, China.

Plos One
|July 11, 2013
PubMed
Summary
This summary is machine-generated.

This study introduces a new method using active learning to select valuable protein data, overcoming training data shortages for improved subcellular localization prediction.

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Last Updated: May 9, 2026

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Protein Science

Background:

  • Protein subcellular localization is crucial for understanding protein function and interactions.
  • Computational methods for predicting protein location often suffer from limited training data.
  • Existing prediction tasks face challenges due to a shortage of experimentally validated protein annotations.

Purpose of the Study:

  • To address the training data shortage in protein subcellular localization prediction.
  • To develop a novel method for mining proteins with non-experimental annotations.
  • To enhance the performance of protein subcellular localization classifiers.

Main Methods:

  • A new strategy employing active learning to select informative samples from proteins with non-experimental annotations.
  • Utilizing non-experimental evidence from protein databases to expand training datasets.
  • Implementing an active sample selection approach to estimate sample value and identify optimal additions to training sets.

Main Results:

  • The proposed method effectively identifies and selects valuable protein samples from a larger pool.
  • Supplementing original training sets with selected samples significantly improves classifier performance.
  • Numerical experiments demonstrated performance gains across four popular multi-label classifiers on benchmark datasets.

Conclusions:

  • The active sample selection strategy successfully mitigates the training data shortage problem.
  • This approach enhances the accuracy and reliability of computational protein subcellular localization prediction.
  • The method offers a valuable tool for improving bioinformatics prediction models.