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Related Concept Videos

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...
Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
Affinity and Avidity01:41

Affinity and Avidity

Overview
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Related Experiment Video

Updated: May 29, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Affinity ligands from chemical combinatorial libraries.

Enrique Carredano1, Herbert Baumann

  • 1GE Healthcare Bio-Sciences AB, SE-751 84 Uppsala, Sweden.

Methods of Biochemical Analysis
|September 30, 2011
PubMed
Summary
This summary is machine-generated.

This study explores identifying small organic molecule affinity ligands for target proteins. While these ligands show lower affinity than natural ones, careful optimization can yield significant purification factors.

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Published on: December 1, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Identifying affinity ligands is crucial for protein purification and drug development.
  • Small organic molecules offer an alternative to traditional protein-based ligands.
  • Understanding ligand-target interactions is key to optimizing purification strategies.

Purpose of the Study:

  • To outline methods for identifying low molecular weight organic molecule affinity ligands for target proteins.
  • To discuss strategies for utilizing available information in different scenarios for ligand identification.
  • To summarize published results on small molecule affinity ligands.

Main Methods:

  • Literature review and data compilation of published studies on small molecule affinity ligands.
  • Analysis of ligand structure, target protein, and experimental conditions.
  • Discussion of optimization strategies for binding and elution.

Main Results:

  • Small molecule affinity ligands were identified for various target proteins.
  • Published cases demonstrate lower selectivity and affinity compared to natural protein ligands.
  • A summary of ligand structures, target proteins, and references is provided in Table 10.1.

Conclusions:

  • Low molecular weight organic molecule affinity ligands can be identified using various approaches.
  • Optimization of binding and elution conditions is essential to overcome lower affinity and achieve effective purification.
  • Further research can enhance the utility of small molecule ligands in biochemical applications.