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Related Concept Videos

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-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 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...
z Scores and Area Under the Curve01:17

z Scores and Area Under the Curve

z scores are the standardized values obtained after converting a normal distribution into a standard normal distribution. A z score is measured in units of the standard deviation. The z score tells you how many standard deviations the value x is above (to the right of) or below (to the left of) the mean, μ. Values of x that are larger than the mean have positive z scores, and values of x that are smaller than the mean have negative z scores. If x equals the mean, then x has a z score of zero.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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Related Experiment Video

Updated: May 11, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

InterEvScore: a novel coarse-grained interface scoring function using a multi-body statistical potential coupled to

Jessica Andreani1, Guilhem Faure, Raphael Guerois

  • 1CEA, iBiTecS, Service de Bioenergetique Biologie Structurale et Mecanismes SB2SM, Laboratoire de Biologie Structurale et Radiobiologie LBSR, F-91191 Gif sur Yvette, France.

Bioinformatics (Oxford, England)
|May 9, 2013
PubMed
Summary
This summary is machine-generated.

InterEvScore, a new scoring function, improves protein interaction prediction by incorporating multi-body interactions and evolutionary data. This method enhances the accuracy of identifying protein interfaces compared to existing scoring functions.

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

  • Computational Biology
  • Structural Bioinformatics
  • Protein Interaction Prediction

Background:

  • Accurate prediction of protein-protein interactions is crucial for understanding biological processes.
  • Existing scoring functions often lack multi-body interactions and evolutionary information, limiting their effectiveness.
  • Protein interfaces are under evolutionary pressure, suggesting evolutionary data can improve prediction.

Purpose of the Study:

  • To develop a novel scoring function, InterEvScore, for improved protein interaction prediction.
  • To integrate multi-body interactions and evolutionary information into a scoring function.
  • To evaluate the performance of InterEvScore against established methods.

Main Methods:

  • Developed InterEvScore, a coarse-grained statistical potential incorporating two- and three-body interactions.
  • Combined the statistical potential with evolutionary information for each residue.
  • Utilized a protein docking benchmark dataset with 54 test cases.

Main Results:

  • InterEvScore significantly improves the discrimination of near-native protein interfaces.
  • The inclusion of evolutionary information progressively enhances the scoring function's discriminative power.
  • InterEvScore outperforms existing scoring functions like ZDOCK, ZRANK, and SPIDER.

Conclusions:

  • InterEvScore represents a significant advancement in scoring functions for protein interaction prediction.
  • The integration of multi-body interactions and evolutionary data is key to improved accuracy.
  • This novel approach offers a more efficient way to identify biologically relevant protein interfaces.