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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.
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Conservation of Protein Domains02:26

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The primary structure of a protein is its amino acid sequence.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Updated: Jun 16, 2026

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Quat-2L: a web-server for predicting protein quaternary structural attributes.

Xuan Xiao1, Pu Wang, Kuo-Chen Chou

  • 1Computer Department, Jing-De-Zhen Ceramic Institute, Jing-De-Zhen, 333001, China. xiaoxuan0326@yahoo.com.cn

Molecular Diversity
|February 12, 2010
PubMed
Summary
This summary is machine-generated.

A new tool, Quat-2L, predicts protein quaternary structure using only amino acid sequences. This predictor identifies oligomer types and subtypes with high accuracy, aiding structural biology research.

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Area of Science:

  • Computational Biology
  • Structural Biology
  • Bioinformatics

Background:

  • Protein quaternary structure is crucial for biological function.
  • Predicting quaternary structure from sequence alone remains a challenge.

Purpose of the Study:

  • To develop a novel computational tool for predicting protein quaternary structural attributes.
  • To accurately classify proteins as monomers, homo-oligomers, or hetero-oligomers.
  • To further identify specific oligomer subtypes (dimer, trimer, etc.).

Main Methods:

  • Hybridization of functional-domain and sequence-correlated pseudo amino acid composition approaches.
  • Development of a two-layer prediction model named Quat-2L.
  • Utilizing jackknife cross-validation on a stringent benchmark dataset.

Main Results:

  • Quat-2L achieved an overall success rate of 71.14% in the first layer (monomer, homo-, or hetero-oligomer identification).
  • The second layer achieved success rates of 76.91% for homo-oligomers and 82.52% for hetero-oligomers.
  • The predictor provides results within approximately 15 seconds.

Conclusions:

  • Quat-2L demonstrates effective prediction of protein quaternary structure using sequence information.
  • The tool offers a rapid and accessible method for structural attribute prediction.
  • Quat-2L is available as a publicly accessible web server.