Impact of Charge State on Characterization of Large Middle-Down Sized Peptides by Tandem Mass Spectrometry
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ABSTRACT: Fragmentation trends of large peptides were characterized by five activation methods, including HCD, ETD, EThcD, 213 nm UVPD and 193 nm UVPD. Sequence coverages and scores were assessed based on charge site, peptide sequence and peptide size. Results from four model peptides, neuromedin, glucagon, galanin and amyloid B, showed a charge state dependence on sequence coverage for collision and electron-based activation methods. The effect of charge state and peptide size on sequence coverage was also explored for a Glu-C digest of E. coli ribosomal proteins, resulting in a maximum sequence coverage between 2-6 kDa depending on the activation method.
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Escherichia Coli (ncbitaxon:562)
SUBMITTER: Jennifer Brodbelt
PROVIDER: MSV000093440 | MassIVE | Mon Nov 20 14:39:00 GMT 2023
REPOSITORIES: MassIVE
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