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Related Concept Videos

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...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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...
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...
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...
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...

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Related Experiment Video

Updated: Jun 25, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

QuatIdent: a web server for identifying protein quaternary structural attribute by fusing functional domain and

Hong-Bin Shen1, Kuo-Chen Chou

  • 1Institute of Image Processing & Pattern Recognition, Shanghai Jiaotong University, 800 Dongchuan Road, Shanghai, 200240, China.

Journal of Proteome Research
|February 20, 2009
PubMed
Summary

A new tool, QuatIdent, accurately predicts protein quaternary structures, distinguishing between monomers and various oligomers. This aids essential biological research and drug discovery by quickly identifying protein complex formations.

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Last Updated: Jun 25, 2026

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

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Published on: November 3, 2011

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

Published on: July 12, 2022

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Proteins function as oligomers with diverse quaternary structures, crucial for biological processes like allostery.
  • The post-genomic era yields vast protein sequences, necessitating efficient quaternary structure identification.

Purpose of the Study:

  • Develop a robust tool for timely identification of protein quaternary structural attributes.
  • Enable accurate prediction of protein oligomeric states for research and drug discovery.

Main Methods:

  • Developed QuatIdent, a 2-layer ensemble predictor.
  • Fused functional domain and sequential evolution information for prediction.
  • Utilized jackknife cross-validation on stringent benchmark datasets.

Main Results:

  • QuatIdent achieved 71.1% accuracy for the first layer (identifying 10 quaternary states).
  • Second layer prediction (homo- vs. hetero-oligomer) ranged from 84% to 96% accuracy.
  • The web server provides results in approximately 25 seconds per query.

Conclusions:

  • QuatIdent is a powerful and accessible tool for predicting protein quaternary structures.
  • Accurate and rapid identification of oligomeric states supports fundamental biological studies and pharmaceutical development.