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Related Concept Videos

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...
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...
Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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 electron 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 behind a...
Protein Dynamics in Living Cells01:19

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Related Experiment Video

Updated: Jun 2, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Capturing protein structural kinetics by mass spectrometry.

Gili Ben-Nissan1, Michal Sharon

  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.

Chemical Society Reviews
|May 7, 2011
PubMed
Summary
This summary is machine-generated.

Structural mass spectrometry (MS) reveals protein dynamics, crucial for biological function. This technique captures slow conformational changes, offering insights into protein folding and interactions over time.

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

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Last Updated: Jun 2, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Understanding protein structure is vital for biological function.
  • Protein dynamics and motion are essential for stability and reactivity.
  • Existing techniques often provide ensemble averages, masking individual state behaviors.

Purpose of the Study:

  • To review structural mass spectrometry (MS) as a method for studying protein dynamics.
  • To highlight MS's ability to capture slow time-scale conformational changes.
  • To discuss the advantages and applications of MS in quantitative kinetic monitoring.

Main Methods:

  • Focus on structural mass spectrometry (MS) for probing protein dynamics.
  • MS captures functional conformational transitions in the millisecond to hour range.
  • MS is a non-ensemble technique, resolving distributions of co-existing states.

Main Results:

  • MS provides sensitive and rapid analysis of protein dynamics.
  • The technique resolves the entire distribution of co-existing protein states within a single spectrum.
  • MS enables quantitative monitoring of structural kinetics.

Conclusions:

  • Structural MS is a powerful tool for understanding protein dynamics.
  • It offers unique insights into processes like protein folding, enzymatic reactions, and ligand binding.
  • MS-based strategies are valuable for studying complex biomolecular pathways.