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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-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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...

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

Published on: November 12, 2012

Identifying protein complexes using hybrid properties.

Lei Chen1, Xiaohe Shi, Xiangyin Kong

  • 1Shanghai Key Laboratory of Trustworthy Computing, East China Normal University, Shanghai 200062, People's Republic of China.

Journal of Proteome Research
|September 22, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a novel computational method to identify yeast protein complexes using hybrid features. Graph features were found to be most crucial for accurately predicting protein complex formation.

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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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Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

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Area of Science:

  • Molecular Biology
  • Computational Biology
  • Bioinformatics

Background:

  • Protein complexes are essential for cellular functions, integrating multiple gene products.
  • Identifying protein complexes computationally often relies on analyzing protein-protein interaction (PPI) networks.
  • Existing methods primarily focus on densely connected regions within PPI graphs.

Purpose of the Study:

  • To develop an alternative computational approach for identifying yeast protein complexes.
  • To determine if multiple yeast proteins can form a protein complex using hybrid features.
  • To evaluate the effectiveness of graph and biological properties in complex prediction.

Main Methods:

  • Utilized a dataset of 493 positive and 9878 negative yeast protein complexes.
  • Represented each complex using graph features and biological properties (protein length, biochemical, physicochemical).
  • Applied Minimum Redundancy Maximum Relevance, Incremental Feature Selection, and Forward Feature Selection for feature optimization.
  • Employed the Nearest Neighbor Algorithm for prediction and jackknife cross-validation for accuracy assessment.

Main Results:

  • Achieved a highest identification accuracy of 69.17% for real protein complexes.
  • Feature analysis revealed that graph features are the primary determinants in protein complex identification.
  • The hybrid feature approach, combined with optimized feature selection, proved effective.

Conclusions:

  • The proposed method offers a viable alternative for identifying protein complexes.
  • Graph-based features are highly significant for understanding protein complex formation.
  • Further research can refine this approach for broader applications in systems biology.