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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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.
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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Related Experiment Video

Updated: Jun 2, 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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SCORER 2.0: an algorithm for distinguishing parallel dimeric and trimeric coiled-coil sequences.

Craig T Armstrong1, Thomas L Vincent, Peter J Green

  • 1School of Chemistry, University of Bristol, Bristol BS8 1TS, UK.

Bioinformatics (Oxford, England)
|May 18, 2011
PubMed
Summary
This summary is machine-generated.

We improved SCORER, an algorithm that predicts coiled-coil protein structures. The updated SCORER outperforms existing methods, especially for short or diverse coiled coils.

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Area of Science:

  • Protein structure and biophysics
  • Bioinformatics and computational biology

Background:

  • Coiled coils are common α-helical protein domains crucial for protein-protein interactions.
  • While sequence analysis is straightforward, coiled coil structures exhibit complex oligomeric states and topologies.
  • Predicting the oligomeric state of coiled coils from their amino acid sequence is a significant challenge.

Purpose of the Study:

  • To improve the accuracy of predicting coiled coil oligomeric states from protein sequences.
  • To develop a superior algorithm for distinguishing between parallel coiled coil dimers and trimers.

Main Methods:

  • The SCORER algorithm was revised with an improved statistical foundation.
  • The SCORER training dataset was expanded and updated using only structurally validated coiled coils.
  • The performance of the revised SCORER was compared against the MultiCoil algorithm.

Main Results:

  • The enhanced SCORER algorithm demonstrates significantly improved performance in predicting coiled coil oligomeric states.
  • SCORER 2.0 outperforms MultiCoil, particularly for predicting the oligomeric state of short coiled coils.
  • The revised algorithm shows greater accuracy for coiled coils that are diverse from the original training set.

Conclusions:

  • The improved SCORER algorithm provides a more accurate method for predicting coiled coil oligomeric states.
  • SCORER 2.0 offers enhanced capabilities for analyzing protein structures, especially for challenging cases.
  • This advancement aids in understanding protein-protein interactions and biological processes mediated by coiled coils.