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Related Concept Videos

Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and signal-to-noise ratio for the analyte. 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 collision-induced...
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Peptide Identification Using Tandem Mass Spectrometry01:33

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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.
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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 Spectrometry: Complex Analysis01:21

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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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Updated: Oct 26, 2025

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Subsecond Time-Resolved Mass Spectrometry in Dynamic Structural Biology.

Cristina Lento1, Derek J Wilson1

  • 1Department of Chemistry, York University, Toronto, Ontario M3J 1P3, Canada.

Chemical Reviews
|July 29, 2021
PubMed
Summary

Subsecond time-resolved mass spectrometry (MS) reveals the dynamic nature of biomolecules, overcoming limitations of static structural biology methods. This technique offers crucial insights into protein function and disease mechanisms.

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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Biomolecular function relies on dynamic structural changes, which are difficult to capture with traditional structural biology techniques like X-ray crystallography, NMR, and cryo-EM.
  • These static methods provide high resolution but are ill-suited for observing molecules in motion.

Purpose of the Study:

  • To review the advancements and applications of subsecond time-resolved mass spectrometry (MS) in dynamic structural biology.
  • To highlight how MS provides insights into the dynamic processes driving biomolecular function and pathogenesis.

Main Methods:

  • Subsecond time-resolved mass spectrometry (MS) is employed to monitor biochemical processes and conformational shifts in real-time.
  • Structural information is derived from electrospray charge-state distribution, ion mobility, covalent labeling, and hydrogen-deuterium exchange.

Main Results:

  • Time-resolved MS has enabled direct monitoring of dynamic events such as protein (mis)folding, complexation, aggregation, ligand binding, and enzyme catalysis.
  • This technique provides a unique window into the conformational free energy landscapes of biomolecules.

Conclusions:

  • Subsecond time-resolved MS is a powerful tool for studying dynamic structural biology, complementing static methods.
  • It offers critical insights into the dynamic drivers of protein function and is essential for understanding biological processes and disease.