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Related Experiment Video

Updated: Jul 11, 2026

Measurement of Ultrafast Vibrational Coherences in Polyatomic Radical Cations with Strong-Field Adiabatic Ionization

Measurement of Ultrafast Vibrational Coherences in Polyatomic Radical Cations with Strong-Field Adiabatic Ionization

Published on: August 6, 2018

Fast atom bombardment mass spectrometry.

Science (New York, N.Y.)

|October 15, 1982

Summary

Fast atom bombardment mass spectrometry (FAB MS) is a powerful technique for analyzing large molecules. It effectively ionizes and detects inorganic clusters and peptides, aiding in structural determination.

Area of Science:

Analytical Chemistry
Spectrometry

Background:

Fast atom bombardment mass spectrometry (FAB MS) emerged as a significant analytical tool in 1981.
It enables ionization of samples in a condensed state, typically within a glycerol matrix.

Purpose of the Study:

To highlight the capabilities of FAB MS as a structural elucidation method.
To showcase its application in analyzing diverse chemical entities.

Main Methods:

Samples are bombarded with high-energy xenon or argon atoms (5000–10,000 eV).
This process generates secondary ions (positive and negative) sputtered from the sample surface.

Main Results:

FAB MS successfully detected inorganic ion clusters up to mass 25,800.

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Analyzing Large Protein Complexes by Structural Mass Spectrometry

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PTR-ToF-MS Coupled with an Automated Sampling System and Tailored Data Analysis for Food Studies: Bioprocess Monitoring, Screening and Nose-space Analysis

PTR-ToF-MS Coupled with an Automated Sampling System and Tailored Data Analysis for Food Studies: Bioprocess Monitoring, Screening and Nose-space Analysis

Published on: May 11, 2017

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Last Updated: Jul 11, 2026

Measurement of Ultrafast Vibrational Coherences in Polyatomic Radical Cations with Strong-Field Adiabatic Ionization

Measurement of Ultrafast Vibrational Coherences in Polyatomic Radical Cations with Strong-Field Adiabatic Ionization

Published on: August 6, 2018

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

PTR-ToF-MS Coupled with an Automated Sampling System and Tailored Data Analysis for Food Studies: Bioprocess Monitoring, Screening and Nose-space Analysis

PTR-ToF-MS Coupled with an Automated Sampling System and Tailored Data Analysis for Food Studies: Bioprocess Monitoring, Screening and Nose-space Analysis

Published on: May 11, 2017

Biologically active peptides were detected up to mass 5700.

Molecular ions were obtained for polar and labile compounds like glycosphingolipids and polyene antibiotics.

Conclusions:

FAB MS is highly effective for determining the structure of complex molecules.
The technique is particularly valuable for sequencing amino acids in polypeptides.
It provides molecular information for challenging sample types previously difficult to analyze.