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Updated: Feb 16, 2026
Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
Published on: November 7, 2019
Defining Noncovalent Ubiquitin Homodimer Interfacial Interactions through Comparisons with Covalently Linked
Nicole D Wagner1, David H Russell1
1Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States.
Abstract:
Covalently linked diubiquitin (diUbq) is known to adopt specific interfacial interactions owing to steric hindrance induced by the covalent tether. K48-linked diUbq preferentially forms hydrophobic interfacial interactions between the two I44 faces under physiological conditions, whereas K63-linked diUbq preferentially forms electrostatic interfacial interactions. Here, we show using collision-induced unfolding ion mobility-mass spectrometry that the recently reported noncovalent dimer of ubiquitin exhibits structural preferences and interfacial interactions that are most similar to that of K48-linked diUbq.
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