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Related Concept Videos

Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

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The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
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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 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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UV–Vis Spectrometers01:14

UV–Vis Spectrometers

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The absorbance of UV and visible (UV–visible) radiations is measured using a UV–visible spectrophotometer. Deuterium lamps, which emit UV radiation, and tungsten lamps, which produce radiation in the visible region, are used as light sources in UV–visible spectrophotometers. A monochromator or prism is used for diffraction grating, i.e., to split the incoming radiation into different wavelengths. A system of slits is used to focus the desired wavelength on the sample cell.
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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

Mass Spectrometry: Complex Analysis

736
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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Updated: Jun 13, 2025

Molecular Beam Mass Spectrometry With Tunable Vacuum Ultraviolet VUV Synchrotron Radiation
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Advancing Protein Analysis: A Low-Pressure Drift Tube Orbitrap Mass Spectrometer for Ultraviolet

Jamie P Butalewicz1, James D Sanders1, Kyle J Juetten1

  • 1Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.

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Ultraviolet photodissociation mass spectrometry combined with ion mobility provides conformationally selective structural information for proteins. This technique analyzes fragment ion arrival times to reveal protein folding and elongation in the gas phase.

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Area of Science:

  • Proteomics
  • Structural Biology
  • Analytical Chemistry

Background:

  • Ultraviolet photodissociation (UVPD) mass spectrometry (MS) is a powerful tool for protein structural characterization.
  • Interpreting UVPD fragmentation patterns offers insights into protein secondary and tertiary structures.
  • Protein complexity and conformational diversity present challenges in structural analysis.

Purpose of the Study:

  • To combine UVPD-MS with drift tube ion mobility for conformationally selective MS/MS analysis.
  • To develop a method for resolving protein conformers using mass spectrometry.
  • To enhance the understanding of gas-phase protein structures.

Main Methods:

  • Integration of UVPD-MS with a low-pressure drift tube (LPDT) Orbitrap mass spectrometer.
  • Utilizing 193 nm UVPD for ion activation and fragmentation.
  • Analysis of arrival time distributions (ATDs) of fragment ions to characterize conformers.

Main Results:

  • The integrated platform enables the analysis of protein conformers via fragment ion ATDs.
  • Comparison of ATDs across different cleavage sites or charge states provides insights into protein folding.
  • Demonstrated potential for obtaining conformationally selective MS/MS data.

Conclusions:

  • The combined UVPD-MS and ion mobility technique offers a novel approach to gas-phase protein structural analysis.
  • This method allows for the investigation of protein folding and elongation.
  • The platform advances the characterization of complex protein structures.