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Related Concept Videos

Phosphodiester Linkages01:01

Phosphodiester Linkages

Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
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: Jun 17, 2026

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
10:49

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Cleavable linker for photo-cross-linked small-molecule affinity matrix.

Naoki Kanoh1, Hiroshi Takayama, Kaori Honda

  • 1Tohoku University, Advanced Science Institute, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. kanoh@mail.pharm.tohoku.ac

Bioconjugate Chemistry
|December 24, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a photoactivatable linker with a cleavable site. This innovation allows for verification of immobilized small molecules and efficient detection of bound proteins on affinity matrices.

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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
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Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

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Last Updated: Jun 17, 2026

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling
10:49

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Affinity Chromatography

Background:

  • Photoactivatable linkers are crucial for immobilizing molecules onto surfaces.
  • Site-nonselective carbene reactions are commonly used for this immobilization.
  • Verifying immobilization and detecting bound targets can be challenging.

Purpose of the Study:

  • To engineer a photoactivatable linker with a cleavable site for improved molecular immobilization.
  • To enable verification of small molecule presence on an affinity matrix.
  • To facilitate efficient detection of proteins covalently bound to immobilized molecules.

Main Methods:

  • Design and synthesis of a novel photoactivatable linker incorporating a cleavable moiety.
  • Utilizing carbene addition/insertion reactions for site-nonselective immobilization of small molecules onto an affinity matrix.
  • Developing methods for verifying the presence of immobilized molecules and detecting bound proteins.

Main Results:

  • Successful incorporation of a cleavable site into the photoactivatable linker.
  • Demonstrated ability to verify the presence of immobilized small molecules on the affinity matrix.
  • Achieved efficient detection of proteins covalently bound to the immobilized small molecules.

Conclusions:

  • The novel cleavable photoactivatable linker enhances the utility of affinity matrices.
  • This linker provides a robust method for verifying molecular immobilization.
  • It significantly improves the detection of protein-ligand interactions.