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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.
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...
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...
Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...
Mass Spectrometry: Carboxylic Acid, Ester, and Amide Fragmentation01:01

Mass Spectrometry: Carboxylic Acid, Ester, and Amide Fragmentation

The fragmentation patterns observed for compounds such as carboxylic acids, esters, and amides in the mass spectra include ⍺-cleavage and McLafferty rearrangement. Fragmentation by ⍺-cleavage preferentially occurs at the carbon-carbon bond at the ⍺-position next to the carboxylic group to generate a neutral radical and a cation. Long chain compounds with hydrogen at their γ-carbon undergo McLafferty rearrangement to give a radical cation and a neutral alkene.
For example, the fragmentation of...
Mass Spectrometry: Molecular Fragmentation Overview01:20

Mass Spectrometry: Molecular Fragmentation Overview

The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can occur at...

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Related Experiment Video

Updated: Jul 14, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

A collision cross-section database of singly-charged peptide ions.

Lei Tao1, Janel R McLean, John A McLean

  • 1The Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A and M University, College Station, College Station, Texas, USA.

Journal of the American Society for Mass Spectrometry
|May 22, 2007
PubMed
Summary

This study presents a database of ion-neutral collision cross-sections for peptide ions, revealing structural insights. Peptide ion mobility measurements show distinct patterns related to enzymatic digestion, aiding structural characterization.

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Synthesis and Mass Spectrometry Analysis of Oligo-peptoids
11:44

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids

Published on: February 21, 2018

Related Experiment Videos

Last Updated: Jul 14, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids
11:44

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids

Published on: February 21, 2018

Area of Science:

  • Analytical Chemistry
  • Biophysical Chemistry
  • Proteomics

Background:

  • Understanding peptide ion structures is crucial for mass spectrometry-based proteomics.
  • Ion mobility spectrometry provides insights into ion size and shape.
  • Enzymatic digestion generates diverse peptide fragments with varying properties.

Purpose of the Study:

  • To create a database of ion-neutral collision cross-sections for singly-charged peptide ions.
  • To correlate collision cross-sections with peptide structure and enzymatic origin.
  • To investigate the relationship between peptide structure and ion mobility measurements.

Main Methods:

  • Peptide ions were generated via enzymatic digestion of proteins using three enzymes.
  • Ion-neutral collision cross-sections were measured using ion mobility spectrometry coupled to time-of-flight mass spectrometry.
  • Matrix-assisted laser desorption ionization (MALDI) was used to form ions at controlled pressures.

Main Results:

  • A database of ion-neutral collision cross-sections for peptide ions was established.
  • Most peptide ions (63%) exhibited charge-solvated globular structures.
  • Significant deviations from globular structures were observed, with trypsin-digested peptides often larger and pepsin-digested peptides often smaller.

Conclusions:

  • Peptide ion collision cross-sections provide valuable structural information.
  • Enzymatic digestion method influences peptide ion structure and mobility.
  • The developed database aids in interpreting ion mobility data for peptide characterization.