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Related Concept Videos

Electrospray Ionization (ESI) Mass Spectrometry01:12

Electrospray Ionization (ESI) Mass Spectrometry

Higher molecular weight biomolecules are nonvolatile compounds that may decompose before ionizing or vaporizing during mass analysis with conventional electron impact ionization methods. Accordingly, electrospray ionization (ESI) is the favored method for vaporizing and ionizing biomolecules as it circumvents rapid fragmentation and enables the recording of mass signals for the entire biomolecule.
ESI utilizes electrical energy to transfer ions from the liquid phase of the sample into the...
Ion-Exchange Chromatography01:09

Ion-Exchange Chromatography

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...
Chemical Ionization (CI) Mass Spectrometry01:21

Chemical Ionization (CI) Mass Spectrometry

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...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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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Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

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Updated: Jul 9, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Conformational and noncovalent complexation changes in proteins during electrospray ionization.

Peter Nemes1, Samita Goyal, Akos Vertes

  • 1Department of Chemistry, W. M. Keck Institute for Proteomics Technology and Applications, George Washington University, Washington, D.C. 20052, USA.

Analytical Chemistry
|December 18, 2007
PubMed
Summary

Electrospray ionization spraying conditions alter protein structures before ionization. Maintaining consistent spraying modes is crucial for accurate protein conformation studies and can be used to study protein folding dynamics.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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Last Updated: Jul 9, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
09:18

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

Published on: April 17, 2017

Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

Analyzing Large Protein Complexes by Structural Mass Spectrometry

Published on: June 19, 2010

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Mass Spectrometry

Background:

  • Electrospray ionization (ESI) is vital for producing gas-phase ions from proteins and their noncovalent complexes.
  • Charge-state distributions of ESI ions are used to infer solution-phase protein conformations.
  • The influence of initial droplet generation conditions on protein structure in ESI remains underexplored.

Purpose of the Study:

  • To investigate how electrospray spraying conditions affect protein and noncovalent complex structures.
  • To determine if initial droplet generation parameters introduce artifacts in conformation studies.
  • To explore the potential of manipulating spraying modes for protein structure studies.

Main Methods:

  • Monitoring spray current and Taylor cone dynamics during electrospray ionization.
  • Utilizing fast imaging techniques to observe droplet generation.
  • Analyzing the charge-state distributions of ions from model proteins (cytochrome c, ubiquitin) and a protein complex (holomyoglobin) under varied spraying modes.

Main Results:

  • Variations in electrospray spraying modes induced conformational changes in proteins and dissociation in protein complexes.
  • Observed structural alterations occurred prior to the ionization process.
  • These changes led to departures from the original secondary, tertiary, and quaternary structures.

Conclusions:

  • Electrospray ionization spraying conditions significantly impact protein and complex structures, potentially creating artifacts in conformation studies.
  • Consistent spraying modes are recommended for accurate correlation between gas-phase and liquid-phase protein conformations.
  • Controlled manipulation of spraying modes offers a novel approach for studying protein folding dynamics.