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Related Concept Videos

Protein Networks02:26

Protein Networks

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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.
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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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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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Conserved Binding Sites01:49

Conserved Binding Sites

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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.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Protein Organization01:24

Protein Organization

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
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Protein Families02:47

Protein Families

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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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A Protocol for Computer-Based Protein Structure and Function Prediction
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A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

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A tensor-based bi-random walks model for protein function prediction.

Sai Hu1, Zhihong Zhang1,2, Huijun Xiong1

  • 1College of Computer Engineering and Applied Mathematics, Changsha University, Changsha, 410022, Hunan, China.

BMC Bioinformatics
|May 31, 2022
PubMed
Summary
This summary is machine-generated.

We developed Random Walks with Restart on Tensor (RWRT) for protein function prediction. RWRT integrates multi-omics data and protein interaction networks, significantly improving prediction accuracy by overcoming noise in existing methods.

Keywords:
Bi-random walksProtein functionProtein–protein interactionTensor

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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Area of Science:

  • Computational biology
  • Bioinformatics
  • Systems biology

Background:

  • Accurate protein function characterization is vital for molecular understanding, impacting biomedicine and pharmaceuticals.
  • Computational protein function prediction has been extensively studied.
  • Integrating multi-omics data with network topologies presents a significant challenge due to noise and errors in protein-protein interaction (PPI) networks.

Purpose of the Study:

  • To develop a novel computational method for accurate protein function prediction.
  • To address the limitations of existing methods in handling noisy PPI networks and integrating diverse biological data.
  • To establish a robust data model for preserving intrinsic characteristics of network topologies and biological data.

Main Methods:

  • Proposed the Random Walks with Restart on Tensor (RWRT) method.
  • Constructed a functional similarity tensor by integrating protein interaction networks with multi-omics data (domain annotation, protein complex information).
  • Extended the bi-random walks algorithm to a tensor framework for scoring protein functional similarity and applied a cohesiveness coefficient for filtering.

Main Results:

  • RWRT significantly outperforms state-of-the-art methods in protein function prediction.
  • Achieved at least an 18% improvement in the area under the receiver-operating curve (AUROC).
  • Demonstrated effective filtering of potential false positives and accurate annotation of target proteins.

Conclusions:

  • A functional similarity tensor provides an effective alternative for integrating diverse network data.
  • The tensor-based random walk model successfully discovers functionally similar proteins and mitigates errors in PPI networks.
  • Effective protein function prediction relies on extracting and leveraging comprehensive functional similarity information from protein correlations.