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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Genome Annotation and Assembly03:36

Genome Annotation and Assembly

The genome refers to all of the genetic material in an organism. It can range from a few million base pairs in microbial cells to several billion base pairs in many eukaryotic organisms. Genome assembly refers to the process of taking the DNA sequencing data and putting it all back together in a correct order to create a close representation of the original genome. This is followed by the identification of functional elements on the newly assembled genome, a process called genome annotation.
Conservation of Protein Domains02:26

Conservation of Protein Domains

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Families02:47

Protein Families

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 locations, protein...
Protein Families02:47

Protein Families

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 locations, protein...
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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Assessment of protein set coherence using functional annotations.

Monica Chagoyen1, Jose M Carazo, Alberto Pascual-Montano

  • 1Centro Nacional de Biotecnología-CSIC, Madrid, Spain. monica.chagoyen@cnb.csic.es

BMC Bioinformatics
|October 22, 2008
PubMed
Summary

This study introduces a new computational method to quantify protein set functional homogeneity. The approach uses statistical testing to validate protein sets, aiding biological interpretation and functional module discovery.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Systems Biology

Background:

  • Large-scale experimental datasets yield protein sets requiring functional interpretation.
  • Existing computational methods analyze functional annotations but lack homogeneity measurement.
  • There is a need for methods to assess the coherence of protein sets.

Purpose of the Study:

  • To present a novel method for scoring the functional homogeneity (coherence) of protein sets.
  • To enable validation of protein sets based on the global similarity of their functional annotations.
  • To provide a computational tool for initial assessment of protein set coherence.

Main Methods:

  • Developed a method to score protein set functional homogeneity based on annotation similarity.
  • Employed statistical hypothesis testing to assess set significance against a reference functional space.
  • Utilized global similarity of functional annotations for coherence scoring.

Main Results:

  • The method successfully scores the degree of functional homogeneity in protein sets.
  • Statistically significant coherence was observed in known biologically relevant sets (e.g., macromolecular complexes, pathways).
  • The approach is useful for validating functional modules derived from protein-protein interaction networks.

Conclusions:

  • The presented method effectively measures protein set functional coherence.
  • The tool aids in the initial validation of protein sets before detailed functional interpretation.
  • The approach is applicable to diverse biological datasets and functional module identification.