Related Experiment Video
Updated: Feb 1, 2026
08:40
Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
Published on: January 20, 2022
4.9K
Differential Ion Mobility Separations/Mass Spectrometry with High Resolution in Both Dimensions
Matthew A Baird1, Gordon A Anderson2, Pavel V Shliaha3
1Department of Chemistry , Wichita State University , 1845 Fairmount , Wichita , Kansas 67260 , United States.
Analytical Chemistry
|December 14, 2018
Summary
High-resolution separation of isomers using differential ion mobility spectrometry (FAIMS) is now possible with nitrogen gas. This breakthrough enables seamless integration with mass spectrometry for detailed biological and environmental analyses.
Area of Science:
- Analytical Chemistry
- Biochemistry
- Spectrometry
Background:
- Differential Ion Mobility Spectrometry (FAIMS) offers orthogonality to mass spectrometry for isomer separation.
- High FAIMS resolution typically requires helium or hydrogen buffers, hindering integration with ultrahigh vacuum mass spectrometers.
- Ultrahigh vacuum mass spectrometry, particularly Fourier Transform Mass Spectrometry (FTMS), provides critical resolution and accuracy for biological and environmental studies.
Purpose of the Study:
- To enable high FAIMS resolution using only nitrogen gas for simplified integration with mass spectrometry platforms.
- To demonstrate the capability of nitrogen-based FAIMS coupled with FTMS for analyzing complex biological samples.
Main Methods:
- Increased waveform amplitude to 6 kV in FAIMS.
- Utilized nitrogen (N₂) as the sole buffer gas.
- Coupled the modified FAIMS system with an Orbitrap XL mass spectrometer equipped with electron transfer dissociation (ETD).
- Evaluated the system's performance using complete histone tails with diverse post-translational modifications.
Main Results:
- Achieved high FAIMS resolution using only nitrogen gas.
- Demonstrated straightforward integration of FAIMS with an Orbitrap XL FTMS system.
- Successfully separated and identified post-translational modification (PTM) localization variants in histone tails.
Conclusions:
- High-voltage FAIMS with nitrogen gas overcomes previous integration limitations with FTMS.
- This approach broadens the applicability of FAIMS-MS for detailed analysis of complex proteomic samples.
- Enables confident identification of PTM localization variants in middle-down proteomics.
Related Concept Videos
01:15High-Resolution Mass Spectrometry (HRMS)
2.5K
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...
2.5K
01:20Separable Differential Equations
88
A separable differential equation is a type of first-order differential equation where the derivative dy/dx can be expressed as a product of two functions: one that depends only on x and another that depends only on y. This allows for the rearrangement of the equation so that all terms involving y are on one side, and all terms involving x are on the other. This process, known as the separation of variables, simplifies the process of solving the equation by enabling the integration of both...
88
01:19Mass Spectrometry: Overview
8.9K
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...
8.9K
01:21Tandem Mass Spectrometry
2.5K
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...
2.5K
01:15Mass Spectrometry of Amines
5.4K
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...
5.4K
01:13Mass Spectrometry: Isotope Effect
4.3K
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...
4.3K