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Related Concept Videos

High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

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The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For...
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Mass Analyzers: Overview01:13

Mass Analyzers: Overview

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The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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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 electrospray 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...
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Mass Spectrometry: Complex Analysis01:21

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.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
1.1K
Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

1.8K
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 low-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...
1.8K
Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

3.1K
Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the difference between the molecular mass. Furthermore, the intensity of these signals is dependent on the...
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Related Experiment Video

Updated: Oct 23, 2025

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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High-Resolution Native Mass Spectrometry.

Sem Tamara1,2, Maurits A den Boer1,2, Albert J R Heck1,2

  • 1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands.

Chemical Reviews
|August 20, 2021
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Summary

Native mass spectrometry (MS) analyzes intact biomolecules, preserving native structures for detailed study. Recent advancements enhance sensitivity and applications in protein analysis and interactions.

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Area of Science:

  • Biochemistry and Biophysics
  • Analytical Chemistry
  • Structural Biology

Background:

  • Native mass spectrometry (MS) is a powerful technique for analyzing intact macromolecules, preserving their native structural features.
  • It allows for the investigation of secondary, tertiary, and quaternary protein structures and other biomolecules.
  • Native MS has rapidly advanced in sensitivity, resolution, and usability over the last decade.

Purpose of the Study:

  • To review recent developments in high-resolution native MS.
  • To highlight novel applications in structural analysis, proteoform profiling, and interaction studies.
  • To showcase the growing impact of native MS in academia and industry.

Main Methods:

  • Utilizing dedicated mass analyzers for enhanced performance.
  • Employing advanced sample preparation and separation techniques.
  • Implementing targeted fragmentation and sophisticated software solutions.

Main Results:

  • Significant improvements in sensitivity and resolving power of native MS.
  • Expansion of applications in structural analysis of protein assemblies.
  • Successful proteoform profiling of biopharmaceuticals and plasma proteins.
  • Quantitative and qualitative analysis of protein-ligand interactions (lipids, drugs, carbohydrates).

Conclusions:

  • High-resolution native MS is a rapidly evolving field with broad applicability.
  • Recent technological advancements have democratized its use and expanded its scope.
  • Native MS is crucial for understanding complex biological systems and developing therapeutics.