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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Published on: October 15, 2018

Nondestructive ion trap mass analysis at high pressure.

Wei Xu, Jeffrey B Maas, Frank J Boudreau

Analytical Chemistry

|December 22, 2010

Summary

High-pressure ion trap mass analysis is now possible using nondestructive image current measurements. This technique enables accurate mass analysis even at pressures above 10 mTorr.

Area of Science:

Analytical Chemistry
Physical Chemistry
Spectroscopy

Background:

Traditional ion trap mass spectrometry is limited by pressure-dependent ion-molecule reactions.
High pressure analysis is challenging due to increased scattering and reduced ion coherence.
Nondestructive analysis methods are desirable for preserving sample integrity.

Purpose of the Study:

To develop a nondestructive method for ion trap mass analysis at high pressures (>1 mTorr).
To adapt image current measurement for high-pressure environments.
To enable mixture analysis and tandem mass spectrometry under these conditions.

Main Methods:

Utilized image current measurement with constant dipolar excitation.
Monitored a harmonic of ion motion instead of secular motion.

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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

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Analyzing Large Protein Complexes by Structural Mass Spectrometry

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Employed narrow band detection coupled with Fourier Transform analysis.

Main Results:

Demonstrated successful mass analysis at pressures of 10 mTorr and higher.
Achieved nondestructive analysis without significant ion loss or fragmentation.
Developed protocols for analyzing complex mixtures and performing tandem mass spectrometry.

Conclusions:

The developed technique offers a viable approach for high-pressure ion trap mass analysis.
Nondestructive analysis at elevated pressures is feasible using image current detection.
This method expands the applicability of ion trap mass spectrometry to new experimental regimes.