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Related Concept Videos

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...
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-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...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jun 20, 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

ANCHOR: web server for predicting protein binding regions in disordered proteins.

Zsuzsanna Dosztányi1, Bálint Mészáros, István Simon

  • 1Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary. zsuzsa@enzim.hu

Bioinformatics (Oxford, England)
|September 1, 2009
PubMed
Summary

ANCHOR predicts protein binding regions that are intrinsically disordered but become ordered upon binding. This web-based tool aids in understanding protein interactions and disorder-to-order transitions.

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Last Updated: Jun 20, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Published on: January 26, 2024

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Published on: July 16, 2017

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

Area of Science:

  • * Biochemistry and Molecular Biology
  • * Bioinformatics and Computational Biology

Background:

  • * Intrinsically disordered proteins (IDPs) play crucial roles in cellular regulation and signaling.
  • * Understanding the binding mechanisms of IDPs is essential for deciphering complex biological processes.

Purpose of the Study:

  • * To introduce ANCHOR, a novel web server for predicting protein binding regions.
  • * To identify regions that are disordered in isolation but transition to an ordered state upon binding.

Main Methods:

  • * Development of a web-based implementation of a novel prediction method.
  • * Integration of the IUPred disorder prediction tool.
  • * Inclusion of simple motif search functionalities.

Main Results:

  • * ANCHOR predicts protein regions capable of disorder-to-order transitions upon binding.
  • * The server provides a user-friendly interface for sequence analysis.

Conclusions:

  • * ANCHOR facilitates the study of protein binding regions involved in disorder-to-order transitions.
  • * The tool is freely available for academic use, promoting research in protein function and regulation.