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Related Experiment Video

Updated: May 26, 2026

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

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

Supercharging protein complexes from aqueous solution disrupts their native conformations.

Harry J Sterling¹, Alexander F Kintzer, Geoffrey K Feld

¹Department of Chemistry, University of California-Berkeley, Berkeley, CA 94720, USA.

Journal of the American Society for Mass Spectrometry

|December 14, 2011

Summary

Aqueous solution supercharging using m-nitrobenzyl alcohol (m-NBA) alters protein complex structures. This technique destabilizes complexes in droplets before ion formation, leading to conformational changes and fragmentation, not just increased charge.

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Published on: October 15, 2018

Area of Science:

Biochemistry
Analytical Chemistry
Structural Biology

Background:

Traveling-wave ion mobility-mass spectrometry (TWIMS-MS) is used to study protein complexes.
Aqueous solution supercharging is a technique to increase ion charge for MS analysis.

Purpose of the Study:

Investigate the impact of aqueous solution supercharging on protein complex structures.
Determine the mechanisms behind supercharging-induced destabilization and fragmentation.

Main Methods:

Traveling-wave ion mobility-mass spectrometry (TWIMS-MS)
Electrospray ionization (ESI) with m-nitrobenzyl alcohol (m-NBA) as a supercharging agent.

Main Results:

Low m-NBA concentrations increased charge on concanavalin A dimers and tetramers.
Higher m-NBA concentrations caused dissociation and increased collision cross section (CCS) of concanavalin A tetramers.
Anthrax toxin octamer complexes destabilized, leading to extensive gas-phase fragmentation, indicating pre-ionization conformational changes.

Conclusions:

Supercharging induces conformational changes in ESI droplets prior to ion formation.
Destabilization is driven by reagent-induced conformational shifts, not solely by increased gas-phase charge.
Supercharging is a powerful tool for probing protein complex stability and structure.