Surface-Induced Dissociation of Anionic vs Cationic Native-Like Protein Complexes.

ABSTRACT: Characterizing protein-protein interactions, stoichiometries, and subunit connectivity is key to understanding how subunits assemble into biologically relevant, multisubunit protein complexes. Native mass spectrometry (nMS) has emerged as a powerful tool to study protein complexes due to its low sample consumption and tolerance for heterogeneity. In nMS, positive mode ionization is routinely used and charge reduction, through the addition of solution additives, is often used, as the resulting lower charge states are often considered more native-like. When fragmented by surface-induced dissociation (SID), charge reduced complexes often give increased structural information over their "normal-charged" counterparts. A disadvantage of solution phase charge reduction is that increased adduction

SUBMITTER: Harvey SR 

PROVIDER: S-EPMC9201936 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature