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Related Concept Videos

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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...
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.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
Mass Spectrometry: Complex Analysis01:21

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.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

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Updated: May 25, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Ion mobility-mass spectrometry for structural proteomics.

Yueyang Zhong1, Suk-Joon Hyung, Brandon T Ruotolo

  • 1Department of Chemistry, University of Michigan, 930 N. University Avenue, Ann Arbor, MI 48109, USA.

Expert Review of Proteomics
|February 2, 2012
PubMed
Summary
This summary is machine-generated.

Ion mobility-mass spectrometry is revolutionizing protein structure analysis, especially for complex assemblies that resist traditional methods. This technique offers rapid structural characterization of protein networks.

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Area of Science:

  • Analytical Chemistry
  • Chemical Physics
  • Biochemistry

Background:

  • Ion mobility coupled to mass spectrometry (IM-MS) is a long-established analytical technique.
  • Its application to protein structure elucidation is a more recent development.
  • IM-MS is increasingly used for protein assemblies that are difficult to study with crystallization or NMR.

Purpose of the Study:

  • To highlight the technology and approaches enabling the use of IM-MS for protein structure analysis.
  • To discuss emerging trends in the field.
  • To showcase the rapid structural characterization of protein networks.

Main Methods:

  • Ion mobility coupled to mass spectrometry (IM-MS).
  • Integration of IM-MS data with classical proteomics approaches (e.g., bottom-up).

Main Results:

  • IM-MS has demonstrated significant potential for interrogating protein and multiprotein complex structures.
  • The technology facilitates structural elucidation of challenging protein assemblies.
  • Emerging trends show successful integration with proteomics for network analysis.

Conclusions:

  • IM-MS is a powerful and increasingly vital tool for protein structural biology.
  • It provides rapid structural characterization of complex protein assemblies and networks.
  • The integration with other proteomics methods enhances its utility.