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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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Protein Networks02:26

Protein Networks

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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.
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Updated: Jan 2, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

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Correction to: Predicting protein inter-residue contacts using composite likelihood maximization and deep learning.

Haicang Zhang1,2, Qi Zhang1,2, Fusong Ju1,2

  • 1Key Lab of Intelligent Information Processing, Institute of Computing Technology, Chinese Academy of Sciences, Beijing, China.

BMC Bioinformatics
|December 1, 2019
PubMed
Summary

The original article contains several errors that have been corrected by the author. These corrections ensure the accuracy of the published scientific findings.

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Area of Science:

  • Corrections to scientific literature
  • Ensuring research integrity

Context:

  • Errors identified in a previously published article
  • Author-initiated corrections

Purpose:

  • To rectify inaccuracies in the original publication
  • To provide a corrected version for readers

Summary:

  • The author has identified and detailed several errors within the original article.
  • A corrigendum will be issued to address these inaccuracies.

Impact:

  • Improved accuracy of the scientific record
  • Enhanced reliability of research findings for the scientific community