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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 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...
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Mass Spectrometers01:16

Mass Spectrometers

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This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:
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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: 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 difference between the molecular mass. Furthermore, the intensity of these signals is dependent on the...
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High-Resolution Mass Spectrometry (HRMS)01:15

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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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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Native Mass Spectrometry: Recent Progress and Remaining Challenges.

Kelly R Karch1,2, Dalton T Snyder2, Sophie R Harvey1,2

  • 1Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, USA;

Annual Review of Biophysics
|January 4, 2022
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Summary
This summary is machine-generated.

Native mass spectrometry (nMS) is a powerful tool for analyzing macromolecular structures. Recent advancements enhance its capabilities for tackling complex biological questions in structural biology.

Keywords:
ion mobilitynative mass spectrometryprotein complexesstructural biology

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Native mass spectrometry (nMS) is a key technique for gas-phase analysis of biomolecular structures and complexes.
  • Understanding macromolecular interactions is crucial in various biological fields.

Purpose of the Study:

  • To review recent advancements in native mass spectrometry (nMS) and related techniques.
  • To highlight the expanding applications of nMS in structural biology.
  • To discuss the complementarity and challenges of nMS in the field.

Main Methods:

  • Review of recent literature on nMS.
  • Discussion of advances in sample preparation, instrumentation, activation methods, and data analysis.
  • Survey of different classes of complexes amenable to nMS analysis.

Main Results:

  • Recent advances have significantly improved the scope and resolution of nMS.
  • nMS is increasingly capable of addressing complex structural biology questions.
  • A wide range of macromolecular complexes can now be studied using nMS.

Conclusions:

  • nMS is a rapidly evolving technique with broad applicability in structural biology.
  • Further developments in instrumentation and analysis will continue to expand its utility.
  • nMS offers valuable complementary data to established structural biology methods.