Top‐down analysis of novel synthetic branched proteins
Year: 2018
Type: article
Abstract: A strategy for top-down analysis of branched proteins has been reported earlier, which relies on electron transfer dissociation assisted by collisional activation, and software designed for graphic interpretation of tandem mass spectra and adapted for branched proteins. In the present study, the strategy is applied to identify unknown and novel products of reactions in which rationally mutated proteoforms of Rub1 are used to probe the selectivity of E1 and E2 enzymes normally active in ubiquitination. To test and demonstrate this application, components and attachment sites of three branched dimers are deduced and the mutations are confirmed.
Source: Journal of Mass Spectrometry
DOI: 10.1002/jms.4303
Institution: University of Maryland, College Park
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: green
Awards: G2645038138, Orbitrap Fusion Tribrid Mass Spectrometer, NSF/MCB-BSF: Cross-activation of ubiquitin and Rub1 to understand their roles as separate protein modifiers, G7392406557, APPLICATIONS OF MASS SPECTROMETRY IN PHARMACOLOGY, Ubiquitinated Proteins in Exosomes of Immune Suppressive Myeloid Cells, G9000053133
OpenAlex ID: W2897196406