Related Experiment Video
Updated: Jul 8, 2026

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
Published on: June 27, 2018
Slice Collision-Induced Unfolding and Molecular Dynamics Reveal How Post-Translational Succination Reshapes SUMO1
Louis Groignet1,2, Thomas Robert1, Quentin Duez1
1Organic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, MonsB-7000, Belgium.
Abstract:
SUMO1 (small ubiquitin-like modifier 1) is a central feature of post-translational SUMOylation, modifying a broad range of substrate proteins. SUMO1 itself is prone to succination, i.e., a post-translational Michael addition of cysteine onto fumarate, which results in the formation of succinated SUMO1 with modified properties. The present study assesses the structural and gas-phase stability modifications in SUMO1 induced by diethyl fumarate succination using advanced ion mobility spectrometry-mass spectrometry (IMS-MS) techniques. Among them, collision-induced unfolding (CIU) and slice-CIU highlight a modified unfolding process resulting from the creation of specific charge-dipole interactions involving the appended dicarbonyl moiety. The experimental results are further supported by molecular dynamics simulations to understand, at the atomistic level, the mechanisms underlying the CIU of gaseous (derivatized) SUMO1 ions.
More Related Videos
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.

