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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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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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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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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...
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A Protocol for Computer-Based Protein Structure and Function Prediction
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Hierarchical ensemble methods for protein function prediction.

Giorgio Valentini1

  • 1AnacletoLab-Dipartimento di Informatica, Università degli Studi di Milano, Via Comelico 39, 20135 Milano, Italy.

ISRN Bioinformatics
|May 5, 2015
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Summary
This summary is machine-generated.

This review explores hierarchical ensemble methods for protein function prediction, addressing challenges like incomplete data and class imbalance. These methods leverage hierarchical relationships for improved accuracy in computational biology.

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Area of Science:

  • Computational biology and bioinformatics.
  • Machine learning applications in genomics and proteomics.

Background:

  • Protein function prediction is a complex multiclass, multilabel classification task with inherent challenges.
  • Issues include incomplete annotations, high-dimensional data integration, class imbalance, and defining negative examples.
  • Hierarchical relationships in functional taxonomies (e.g., Gene Ontology, FunCat) necessitate hierarchy-aware methods.

Purpose of the Study:

  • To comprehensively review hierarchical methods for protein function prediction.
  • Focus on ensemble learning machines that incorporate hierarchical class structures.
  • Discuss existing computational methods, their characteristics, advantages, and limitations.

Main Methods:

  • Review of hierarchical ensemble methods for protein function prediction.
  • Ensemble approach: training separate learning machines for specific functional terms.
  • Consensus decision-making that integrates hierarchical class relationships.

Main Results:

  • Hierarchical methods demonstrate significantly better performance than 'flat' hierarchical-unaware methods.
  • Discussion highlights the strengths and weaknesses of various hierarchical ensemble techniques.
  • Identification of key challenges and limitations in current protein function prediction approaches.

Conclusions:

  • Hierarchical ensemble methods are crucial for accurate protein function prediction.
  • Addressing data incompleteness, imbalance, and high dimensionality remains critical.
  • Future research should focus on novel perspectives to overcome existing open problems in the field.