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Related Concept Videos

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Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
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Related Experiment Video

Updated: Jun 11, 2026

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

An isotopically coded CID-cleavable biotinylated cross-linker for structural proteomics.

Evgeniy V Petrotchenko1, Jason J Serpa, Christoph H Borchers

  • 1University of Victoria-Genome British Columbia Proteomics Centre, Department of Biochemistry and Microbiology, University of Victoria, Vancouver Island Technology Park Victoria, British Columbia, Canada.

Molecular & Cellular Proteomics : MCP
|July 13, 2010
PubMed
Summary
This summary is machine-generated.

A new cross-linker, cyanurbiotindipropionylsuccinimide (CBDPS), aids structural proteomics by enabling affinity enrichment and isotopic coding for precise peptide cross-link identification. This method enhances mass spectrometry analysis for complex protein structures.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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

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Published on: March 9, 2010

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Proteomics
  • Structural Biology
  • Biochemistry

Background:

  • Mass spectrometry-based structural proteomics requires specialized cross-linking reagents.
  • Challenges include detecting and assigning cross-links accurately.
  • Affinity enrichment, isotopic coding, and cross-linker cleavage improve peptide cross-link analysis.

Purpose of the Study:

  • To introduce a novel cross-linker, cyanurbiotindipropionylsuccinimide (CBDPS).
  • To demonstrate CBDPS's utility in affinity enrichment, isotopic coding, and CID cleavage for mass spectrometry.
  • To facilitate the identification of interpeptide cross-links in complex protein structures.

Main Methods:

  • Development and application of cyanurbiotindipropionylsuccinimide (CBDPS) cross-linker.
  • Utilizing avidin affinity enrichment to isolate cross-linked peptides.
  • Employing isotopic coding and CID cleavage for MS/MS spectral analysis.
  • Developing software for automated analysis of cross-link spectra.

Main Results:

  • CBDPS enables efficient affinity enrichment of cross-linked peptides using avidin.
  • Isotopic coding and CID cleavage allow differentiation of labeled fragments in MS/MS spectra.
  • Automated analysis facilitated rapid determination of cross-link type and peptide identification.
  • Successful characterization of CBDPS performance on HIV reverse transcriptase.

Conclusions:

  • CBDPS combined with affinity enrichment, isotopic coding, and CID cleavage enables in-depth mass spectrometric analysis of peptide cross-links.
  • This approach overcomes limitations in detecting and assigning cross-links in structural proteomics.
  • The method significantly enhances the identification of interpeptide cross-links.