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Chemical Ionization (CI) Mass Spectrometry01:21

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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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Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
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Phase Transitions: Melting and Freezing02:39

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Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...
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The Collision Theory
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Mass Spectrometry: Molecular Fragmentation Overview01:20

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The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
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Cyclic Ion Mobility-Collision Activation Experiments Elucidate Protein Behavior in the Gas Phase.

Charles Eldrid1, Aisha Ben-Younis1, Jakub Ujma2

  • 1Institute of Structural and Molecular Biology, Division of Bioscience, University College London, London, WC1E 6BT, U.K.

Journal of the American Society for Mass Spectrometry
|May 19, 2021
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Summary
This summary is machine-generated.

Tandem ion mobility mass spectrometry (IM-MS) reveals detailed protein unfolding pathways. This advanced technique analyzes protein dynamics and structural changes, offering new insights into complex biological systems.

Keywords:
ion-mobility mass spectrometryprotein unfolding

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Analytical Chemistry

Background:

  • Ion mobility coupled to mass spectrometry (IM-MS) is a powerful tool for gas-phase protein structure and dynamics.
  • Protein unfolding can be induced by increasing ion energy in the IM cell, yielding insights into proteoform energetics.
  • Cyclic IM-mass spectrometry (cIM-MS) enables multiple, consecutive tandem IM experiments (IMⁿ).

Purpose of the Study:

  • To describe a tandem IM technique for detailed protein unfolding pathways and disordered protein dynamics.
  • To apply this IMⁿ-MS method to model proteins like cytochrome C and human islet amyloid polypeptide (hIAPP).

Main Methods:

  • Utilized a tandem IM technique involving multiple rounds of IM separation and collision activation (CA): IM-CA-IM and CA-IM-CA-IM.
  • Applied the IMⁿ-MS method to cytochrome C and dimeric hIAPP.
  • Analyzed unfolding events and structural interconversions.

Main Results:

  • Observed multiple unfolding events for cytochrome C, consistent with previous IM-MS studies.
  • Detected interconversion between compact and extended structures for both cytochrome C and hIAPP using IMⁿ-MS.
  • hIAPP data indicated conformational interconversion prior to dissociation, suggesting low energy barriers.

Conclusions:

  • Tandem IM techniques (IMⁿ-MS) provide detailed insights into protein unfolding pathways and dynamics.
  • The method is effective for studying complex proteins and peptides, including amyloidogenic ones.
  • Conformational flexibility and low energy barriers play a role in the dynamics of proteins like hIAPP.