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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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...
Complexometric Titration: Ligands00:43

Complexometric Titration: Ligands

Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...

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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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Advancing Collision-Induced Affinity Selection Mass Spectrometry for Quantitative Ligand Analysis in Complex

Xinru Xue1, Ronald J Quinn1, Bernd H A Rehm1,2

  • 1Institute for Biomedicine and Glycomics, Griffith University, Southport, 4215 Gold Coast, Queensland, Australia.

Analytical Chemistry
|March 3, 2026
PubMed
Summary

Collision-Induced Affinity Selection MS (CIAS-MS) offers enhanced detection and affinity ranking of protein-ligand interactions. This optimized platform accurately ranks ligands even in complex biological samples.

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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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07:33

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12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Native mass spectrometry (MS) allows studying protein-ligand interactions in solution.
  • Collision-Induced Affinity Selection MS (CIAS-MS) enhances ligand detection and complex dissociation analysis.
  • Existing methods face limitations in complex biological backgrounds.

Purpose of the Study:

  • To optimize the CIAS-MS platform for improved ligand binding detection and affinity ranking.
  • To integrate positive and negative ion modes for broader ligand detection.
  • To introduce a robust parameter for quantitative affinity ranking.

Main Methods:

  • Utilized optimized Collision-Induced Affinity Selection MS (CIAS-MS) platform.
  • Integrated positive and negative ion modes for comprehensive ligand analysis.
  • Introduced the collision-induced dissociation (CID) slope for affinity ranking.

Main Results:

  • The dual ion mode approach broadened the detection of diverse ligands.
  • The CID slope parameter accurately ranked ligand affinities in solution-phase.
  • CIAS-MS demonstrated robustness in complex mixtures and bacterial lysates.

Conclusions:

  • Optimized CIAS-MS provides robust detection and accurate affinity ranking of protein-ligand interactions.
  • The CID slope is a reliable metric for affinity order, even in challenging samples.
  • CIAS-MS is a scalable platform for high-throughput ligand discovery and proteome-wide studies.