Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes.

ABSTRACT: As applications in mass spectrometry continue to expand into the field of structural biology, there have been an increasing number of studies on noncovalent biological assemblies. Ensuring that protein complexes maintain native-like conformations and architectures during the transition from solution to the gas phase is a key aim. Probing composition and arrangement of subunits of multi-charged complexes via tandem mass spectrometry (MS/MS) may lead to protein unfolding and the redistribution of charges on the constituent subunits, leading to asymmetric charge partitioning and ejection of a high-charged monomer. Additionally, the overall dissociation efficiency of many ion activation methods is often suppressed for low charge states, hindering the effectiveness of MS/MS for complexes that h

SUBMITTER: Sipe SN 

PROVIDER: S-EPMC6580417 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature