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Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF

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Time-Resolved Study of In Situ Generated Protein Subcomplexes by Tandem-Trapped Ion Mobility Spectrometry.

Thais Pedrete¹, Christian Bleiholder^1,2, Fanny C Liu¹

¹Department of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida, USA.

Journal of Mass Spectrometry : JMS

|January 29, 2026

Summary

This summary is machine-generated.

Tandem-trapped ion mobility spectrometry (Tandem-TIMS) enables in situ generation and stability assessment of protein subcomplexes. This advanced method reveals high kinetic stability of streptavidin subunits in the gas phase.

Keywords:

collision‐induced dissociation protein subcomplexes tandem‐ion mobility spectrometry tandem‐trapped ion mobility spectrometry time‐resolved

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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

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Published on: July 31, 2010

Area of Science:

Biochemistry
Analytical Chemistry
Structural Biology

Background:

Native protein complexes are challenging to analyze structurally in the gas phase.
Tandem-TIMS offers unique capabilities for ion manipulation and analysis.

Purpose of the Study:

To develop and apply an advanced analytical strategy using Tandem-TIMS.
To investigate the gas-phase kinetic stability and structural integrity of protein subcomplexes.
To generate and analyze streptavidin subunits from native-like tetramers.

Main Methods:

Utilized tandem-trapped ion mobility spectrometry (Tandem-TIMS) for high-resolution separation.
Employed targeted collisional activation (CID) for controlled dissociation of protein complexes.
Performed in situ generation and gas-phase trapping of protein subcomplexes.

Main Results:

Successfully generated streptavidin monomers, dimers, and trimers from tetramers (15+) via CID.
Demonstrated high kinetic stability of generated streptavidin subcomplexes through extended gas-phase trapping (up to 10.3 s).
Observed unchanged collision cross-section distributions, confirming structural integrity.

Conclusions:

Tandem-TIMS is a versatile platform for advanced, mobility-resolved measurements.
The study provides new structural and kinetic insights into protein complexes in the gas phase.
The method enables direct evaluation of kinetic stability and structural integrity of in situ generated subcomplexes.