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Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Updated: Jan 17, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

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Published on: May 2, 2019

In Cellulo Cysteine Umpolung for Protein Structure Probing.

Philipp Hartmann^1,2, Kostiantyn Bohdan^1,2, Lara Vogelsang³

¹Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany.

Journal of the American Chemical Society

|September 19, 2025

Summary

This summary is machine-generated.

Vinyl thianthrenium tetrafluoroborate (VTT) enables single-step, in-cell protein cross-linking by rapidly forming electrophilic episulfonium ions from native cysteinyl thiols. This method efficiently labels proteins intracellularly for structure prediction.

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

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

Published on: October 15, 2018

Area of Science:

Chemical Biology
Proteomics
Structural Biology

Background:

Intramolecular cross-linking of amino acids is crucial for probing protein structure.
Existing methods like carbene insertion require two steps, while bifunctional electrophiles have limitations in capturing transient protein conformations.
A single-step, in situ cross-linking strategy is needed for efficient protein structure analysis.

Purpose of the Study:

To introduce a novel single-step cross-linking strategy using vinyl thianthrenium tetrafluoroborate (VTT).
To demonstrate the efficiency and speed of VTT-mediated cross-linking within living cells.
To highlight VTT's utility for proteome-wide protein structure determination.

Main Methods:

Utilized vinyl thianthrenium tetrafluoroborate (VTT) for a single-step cross-linking reaction.
Leveraged the umpolung of native cysteinyl thiols to generate electrophilic episulfonium ions.
Performed cross-linking reactions in various cell types and compared with existing reagents (maleimide, iodoacetamide).

Main Results:

VTT mediates rapid (within minutes) in situ cross-linking of amino acids in diverse cell types.
VTT exhibits fast cellular uptake, enabling efficient intracellular labeling even in the presence of competing reagents.
The reaction forms stable ethylene linkers between cysteine and nucleophilic amino acids.

Conclusions:

VTT provides a facile and efficient single-step method for in cellulo protein cross-linking.
The rapid generation of episulfonium ions without exogenous activation facilitates structure prediction.
This approach offers a valuable tool for generating quantitative proteome-wide structural information.