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Related Concept Videos

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,...
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,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Quantification of protein group coherence and pathway assignment using functional association.

Meghana Chitale1, Shriphani Palakodety, Daisuke Kihara

  • 1Department of Computer Science, Purdue University, 305 N, University Street, West Lafayette, Indiana 47907, USA.

BMC Bioinformatics
|September 21, 2011
PubMed
Summary

We developed two novel scores to quantify functional coherence in protein sets, outperforming existing methods in identifying biologically relevant groups and protein interactions. These scores accurately assign proteins to biological pathways.

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Systems Biology

Background:

  • Genomics and proteomics generate vast datasets requiring functional interpretation.
  • Identifying functional units of proteins with coherent roles is crucial for data analysis.
  • Existing functional similarity measures may not adequately capture functional coherence.

Purpose of the Study:

  • To develop novel scores for quantifying functional coherence in protein sets.
  • To assess the performance of these scores in identifying biologically relevant protein groups.

Main Methods:

  • Designed two scores based on Gene Ontology (GO) term associations from protein annotations and PubMed literature.
  • Normalized GO term co-occurrences using a method adapted from protein structure prediction.
  • Evaluated scores against existing functional similarity measures.

Main Results:

  • The developed scores accurately identify functionally coherent protein sets, including pathways, co-localized proteins, and complexes.
  • Scores demonstrate higher accuracy than existing methods for identifying functional units.
  • The scores effectively detect interacting protein pairs and assign proteins to pathways.

Conclusions:

  • Two novel scores for quantifying protein functional coherence have been developed.
  • These scores leverage GO term associations from annotations and literature.
  • The scores show strong performance in distinguishing relevant protein groups, detecting interactions, and assigning proteins to pathways.