Defining Noncovalent Ubiquitin Homodimer Interfacial Interactions through Comparisons with Covalently Linked Diubiquitin
Non-covalent interactions
Hydrophobic effect
Static electricity
DOI:
10.1021/jacs.6b09829
Publication Date:
2016-12-15T00:26:27Z
AUTHORS (2)
ABSTRACT
Covalently linked diubiquitin (diUbq) is known to adopt specific interfacial interactions owing steric hindrance induced by the covalent tether. K48-linked diUbq preferentially forms hydrophobic between two I44 faces under physiological conditions, whereas K63-linked electrostatic interactions. Here, we show using collision-induced unfolding ion mobility-mass spectrometry that recently reported noncovalent dimer of ubiquitin exhibits structural preferences and are most similar diUbq.
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