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Related Concept Videos

Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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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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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 Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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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.
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Related Experiment Video

Updated: Dec 9, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
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ProtFold-DFG: protein fold recognition by combining Directed Fusion Graph and PageRank algorithm.

Jiangyi Shao1, Bin Liu2

  • 1School of Computer Science and Technology, Beijing Institute of Technology, China.

Briefings in Bioinformatics
|September 6, 2020
PubMed
Summary

We introduce ProtFold-DFG, a novel network-based predictor for protein fold recognition. This method improves accuracy by fusing ranking lists using a Directed Fusion Graph (DFG) and PageRank, outperforming 35 existing methods.

Keywords:
Directed Fusion GraphKL divergencePageRankprotein fold recognitiontransitive closure

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Area of Science:

  • Computational biology
  • Bioinformatics
  • Structural biology

Background:

  • Protein fold recognition is crucial for protein structure prediction.
  • Existing computational methods have limitations.
  • Machine learning and AI have advanced prediction techniques.

Purpose of the Study:

  • To develop a novel and accurate computational predictor for protein fold recognition.
  • To address limitations of current protein fold recognition methods.

Main Methods:

  • Proposed a network-based predictor, ProtFold-DFG.
  • Introduced Directed Fusion Graph (DFG) to fuse ranking lists from multiple methods.
  • Utilized transitive closure and KL divergence within the DFG for enhanced generalization.
  • Applied the PageRank algorithm on the DFG to leverage global protein interactions.

Main Results:

  • ProtFold-DFG demonstrated superior performance on the LINDAHL dataset.
  • Outperformed 35 competing protein fold recognition methods.
  • Indicated improved generalization ability and accuracy in fold recognition.

Conclusions:

  • ProtFold-DFG is a highly effective method for protein fold recognition.
  • The Directed Fusion Graph approach enhances prediction accuracy by considering global protein interactions.
  • ProtFold-DFG offers a valuable tool for the scientific community.