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Related Concept Videos

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.
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Tandem Mass Spectrometry01:21

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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 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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Mass Spectrometry of Amines01:15

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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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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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MALDI-TOF Mass Spectrometry01:19

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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...
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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Standard Proteoforms and Their Complexes for Native Mass Spectrometry.

Luis F Schachner1, Ashley N Ives1, John P McGee1

  • 1Departments of Chemistry and Molecular Biosciences, the Chemistry of Life Processes Institute, and the Proteomics Center of Excellence, Northwestern University, 2170 Tech Dr., Silverman Hall, Evanston, IL, 60208, USA.

Journal of the American Society for Mass Spectrometry
|April 10, 2019
PubMed
Summary
This summary is machine-generated.

This study introduces a standard operating procedure for native mass spectrometry (nMS) of proteins. It provides protein standards to improve instrument performance and data reproducibility in proteomics research.

Keywords:
Multi-proteoform complexesNative mass spectrometryNative top-down mass spectrometryProteoformsRigor and reproducibilityStandards

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Area of Science:

  • Analytical Chemistry
  • Structural Biology
  • Proteomics

Background:

  • Native mass spectrometry (nMS) is crucial for analyzing protein assemblies but lacks standardization.
  • Technical challenges hinder instrument operation, benchmarking, and consistent data quality.

Purpose of the Study:

  • To establish a standard operating procedure for high-quality native mass spectrometry (nMS) of proteins.
  • To introduce protein standards for training and assessing instrument performance.
  • To promote normalization and reproducibility in nMS practices.

Main Methods:

  • Developed a standard operating procedure for Orbitrap mass spectrometry.
  • Included reproducible sample preparation, loading, ionization, and analysis steps.
  • Utilized two proteoforms and three complexes as potential standards.

Main Results:

  • Provided a detailed protocol for acquiring native mass spectra of 30-300 kDa proteins.
  • Identified five standards (two proteoforms, three complexes) for instrument benchmarking.
  • Generated spectral data to guide instrument parameter assessment and data analysis.

Conclusions:

  • The developed protocol and standards aim to normalize nMS practices across laboratories.
  • This initiative will enhance reproducibility and ensure high-quality data production in nMS.
  • Facilitates longitudinal assessment of instrument performance and data integrity.