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Tandem Mass Spectrometry

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...

Mass Spectrometry: Complex Analysis

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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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MALDI-TOF Mass Spectrometry

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...

Mass Spectrum: Interpretation

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An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...

Mass Spectrometers

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This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:

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Updated: May 30, 2026

Untargeted Metabolomics from Biological Sources Using Ultraperformance Liquid Chromatography-High Resolution Mass Spectrometry (UPLC-HRMS)

Untargeted Metabolomics from Biological Sources Using Ultraperformance Liquid Chromatography-High Resolution Mass Spectrometry (UPLC-HRMS)

Published on: May 20, 2013

Top-down mass spectrometry: recent developments, applications and perspectives.

Weidong Cui¹, Henry W Rohrs, Michael L Gross

¹NIH NCRR Center for Biomedical and Bio-Organic Mass Spectrometry, Department of Chemistry, Washington University, St. Louis, MO 63130, USA. cui@wustl.edu

|August 10, 2011

Summary

This summary is machine-generated.

Top-down mass spectrometry analyzes intact proteins, offering insights into modifications and complexes. This emerging proteomics strategy contrasts with traditional bottom-up methods for comprehensive biomolecule analysis.

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Area of Science:

Proteomics and Mass Spectrometry
Biomolecular Analysis

Background:

Traditional mass spectrometry focused on intact molecules.
Bottom-up mass spectrometry analyzes peptide fragments after protein digestion.
Top-down mass spectrometry offers an alternative for intact biomolecule analysis.

Purpose of the Study:

To provide an overview of top-down mass spectrometry methodologies.
To review applications of top-down mass spectrometry.
To discuss challenges and future directions in the field.

Main Methods:

Top-down mass spectrometry for intact protein analysis.
Analysis of peptide fragments via bottom-up mass spectrometry for comparison.
Mass spectrometric techniques applied to large biomolecules, protein assemblies, and complexes.

Main Results:

Top-down mass spectrometry is effective for analyzing intact proteins.
Applications include studying protein posttranslational modifications and biophysics.
The approach is also applicable to DNA/RNA and protein assemblies.

Conclusions:

Top-down mass spectrometry is a powerful, emerging technique in proteomics.
It complements traditional methods by analyzing intact biomolecules.
Further development holds promise for advancing biomolecular research.