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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...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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...
Types Of Column Chromatography01:29

Types Of Column Chromatography

The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
Gel Filtration Chromatography
When 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...

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Updated: May 30, 2026

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
08:40

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

Published on: March 14, 2016

[Ligand screening in affinity chromatography and its applications].

Rui Zhao1, Guoquan Liu

  • 1Lab of Analytical Chemistry for Life Science, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.

Se Pu = Chinese Journal of Chromatography
|June 22, 2007
PubMed
Summary
This summary is machine-generated.

Researchers developed a simpler, effective method using antisense peptide libraries to screen for affinity ligands, reducing synthesis and screening efforts for novel purification techniques.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Analytical Chemistry

Context:

  • Affinity chromatography is crucial for selective compound purification.
  • Selecting effective affinity ligands is key for developing new chromatography methods.
  • Conventional screening methods can be complex and time-consuming.

Purpose:

  • To summarize recent advances in affinity ligand selection and screening.
  • To introduce a novel, more efficient screening strategy using antisense peptide libraries.
  • To demonstrate the application of this new method in various biological contexts.

Summary:

  • A new screening method employing antisense peptide-based combinatorial peptide libraries has been developed for identifying affinity ligands.
  • This strategy significantly simplifies and enhances the efficiency of ligand discovery compared to traditional methods.
  • The method facilitates easier structural determination of identified ligands.

Impact:

  • Successfully applied to screen for inhibitors of influenza A virus and SARS coronavirus.
  • Enabled the construction of a quartz crystal microbalance (QCM) biosensor for human interferon-beta.
  • Offers a more streamlined approach for developing affinity chromatography and biosensing applications.