Evidence for Many Resolvable Structures within Conformation Types of Electrosprayed Ubiquitin Ions
Citations Over TimeTop 10% of 2006 papers
Abstract
A new two-dimensional ion mobility spectrometry approach combined with mass spectrometry has been used to examine ubiquitin ions in the gas phase. In this approach ions are separated in an initial drift tube into conformation types (defined by their collision cross sections) and then a gate is used to introduce a narrow distribution of mobility-separated ions into a second drift tube for subsequent separation. The results show that upon selection a narrow peak shape is retained through the second drift tube. This requires that at 300 K the selected distribution does not interconvert substantially within the broader range of structures associated with the conformation type within the approximately 10-20 ms time scale of these experiments. For the [M + 7H]7+ ion, it appears that many ( approximately 5-10) narrow selections can be made across each of the compact, partially-folded, and elongated conformer types, defined previously (Int. J. Mass Spectrom. 1999, 187, 37-47).
Related Papers
- → Activating the ubiquitin family: UBA6 challenges the field(2008)134 cited
- → Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast(2011)9 cited
- → Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria(2021)4 cited
- LJbiquitin--Proteasome System in ABA Signaling: From Perception to Action(2016)
- Cloning and Characterization of DULP, a Novel Ubiquitin-Like Molecule from Human Dendritic Cells(2009)