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Related Concept Videos

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 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...
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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 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...
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Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

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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 mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

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The molecular ion peak of a molecule in the mass spectrum provides vital information for molecular identification. However, conventional electron impact ionization can lead to the rapid dissociation of some molecular ions before they reach the detector. A milder ionization method is required to increase the lifetime of such ionized analyte molecules. Chemical ionization (CI) is a gas-phase protonation reaction useful for mass-analyzing analyte molecules that are easily protonated to yield the...
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Mass Spectrometry: Alkene Fragmentation00:59

Mass Spectrometry: Alkene Fragmentation

3.6K
Alkenes lose one electron from the unsaturated π bond upon ionization and form stable molecular ions. Further fragmentation of alkenes occurs through three different reaction pathways. The most prominent fragmentation is the cleavage at the allylic position. The resultant allylic carbocation is resonance stabilized. In the mass spectra of terminal alkenes, this fragment appears at a mass-to-charge ratio of 41. In the internal alkenes, where there are two choices of allylic cleavage, the...
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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Protein Dynamics in Solution by Quantitative Crosslinking/Mass Spectrometry.

Zhuo A Chen1, Juri Rappsilber2

  • 1Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany.

Trends in Biochemical Sciences
|October 16, 2018
PubMed
Summary

Quantitative crosslinking/mass spectrometry (QCLMS) reveals protein dynamics in solution. This method offers valuable biological insights by studying transient protein interactions in native environments.

Keywords:
crosslinking/mass spectrometryinteractionsprotein conformational changesprotein dynamicsquantitation

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Cellular processes rely on dynamic protein structures and interactions.
  • Studying transient protein dynamics in solution is challenging for traditional methods.
  • Quantitative crosslinking/mass spectrometry (QCLMS) addresses these limitations.

Purpose of the Study:

  • To provide an overview of the current state of QCLMS.
  • To discuss available QCLMS workflows and their applications.
  • To highlight remaining challenges in the field.

Main Methods:

  • Quantitative crosslinking/mass spectrometry (QCLMS) is a key technique.
  • Recent advancements fuse CLMS with quantitative proteomics.
  • The method allows for high-resolution study of protein dynamics in solution.

Main Results:

  • QCLMS enables the study of protein dynamics in solution.
  • The technique provides valuable biological insights.
  • Investigations can be extended to native biological environments.

Conclusions:

  • QCLMS is a powerful tool for studying protein dynamics.
  • The fusion with quantitative proteomics has advanced the field.
  • Further development is needed to address remaining challenges.