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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-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 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,...
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...
Modern Molecular Taxonomy01:29

Modern Molecular Taxonomy

Advancements in molecular biology have revolutionized the identification and characterization of bacteria, with multiple methods leveraging DNA sequencing for enhanced precision. As sequencing technologies improve and costs decline, these approaches are increasingly used in clinical, environmental, and evolutionary studies.Multilocus Sequence Typing (MLST) examines several housekeeping genes, essential chromosomal genes encoding cellular functions, to distinguish strains. Approximately...
Conserved Binding Sites01:49

Conserved Binding Sites

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 analyses the...

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Related Experiment Video

Updated: May 22, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Profile-based short linear protein motif discovery.

Niall J Haslam1, Denis C Shields

  • 1Complex and Adaptive Systems Laboratory, University College Dublin, Ireland.

BMC Bioinformatics
|May 22, 2012
PubMed
Summary

Profile-based methods enhance protein motif discovery, especially in disordered regions. Evolutionary weighting and masking improve performance, complementing existing regular expression techniques for broader motif identification.

Area of Science:

  • Bioinformatics
  • Computational Biology
  • Proteomics

Background:

  • Short linear motifs (SLiMs) are key functional sites in proteins, often found in disordered regions.
  • Existing methods for SLiM discovery primarily use regular expressions.
  • Profile-based methods offer a more detailed representation of motifs.

Purpose of the Study:

  • To evaluate and improve profile-based motif discovery methods for disordered protein regions.
  • To compare profile-based methods with regular expression-based methods.

Main Methods:

  • Applied the MEME (Motif-based Sequence Analysis) algorithm, a profile-based method.
  • Incorporated evolutionary weighting to account for protein homology.
  • Masked poorly conserved regions within disordered proteins.

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Last Updated: May 22, 2026

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Main Results:

  • Unweighted MEME performed poorly on disordered protein motifs.
  • Evolutionary weighting and masking improved MEME's performance to match regular expression methods.
  • Both profile-based and regular expression methods identified distinct sets of motifs.

Conclusions:

  • Profile-based motif discovery methods are a valuable complement to regular expression methods.
  • Despite higher computational cost, profile-based methods can uncover motifs missed by other approaches.
  • Optimized profile-based methods enhance the discovery of functionally important protein motifs.