<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Panczyk EM</submitter><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><funding>NIH HHS</funding><pagination>5513-5520</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8168055</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>93(13)</volume><pubmed_abstract>Native mass spectrometry (nMS), particularly in conjunction with gas-phase ion mobility spectrometry measurements, has proven useful as a structural biology tool for evaluating the stoichiometry, conformation, and topology of protein complexes. Here, we demonstrate the combination of trapped ion mobility spectrometry (TIMS) and surface-induced dissociation (SID) on a Bruker SolariX XR 15 T FT-ICR mass spectrometer for the structural analysis of protein complexes. We successfully performed SID on mobility-selected protein complexes, including the streptavidin tetramer and cholera toxin B with bound ligands. Additionally, TIMS-SID was employed on a mixture of the peptides desArg1 and desArg9 bradykinin to mobility-separate and identify the individual peptides. Importantly, results show that </pubmed_abstract><journal>Analytical chemistry</journal><pubmed_title>Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry.</pubmed_title><pmcid>PMC8168055</pmcid><funding_grant_id>S10 OD018507</funding_grant_id><funding_grant_id>P41GM128577</funding_grant_id><funding_grant_id>P41 GM128577</funding_grant_id><pubmed_authors>Wysocki VH</pubmed_authors><pubmed_authors>Snyder DT</pubmed_authors><pubmed_authors>Panczyk EM</pubmed_authors><pubmed_authors>Park MA</pubmed_authors><pubmed_authors>Ridgeway ME</pubmed_authors><pubmed_authors>Somogyi A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry.</name><description>Native mass spectrometry (nMS), particularly in conjunction with gas-phase ion mobility spectrometry measurements, has proven useful as a structural biology tool for evaluating the stoichiometry, conformation, and topology of protein complexes. Here, we demonstrate the combination of trapped ion mobility spectrometry (TIMS) and surface-induced dissociation (SID) on a Bruker SolariX XR 15 T FT-ICR mass spectrometer for the structural analysis of protein complexes. We successfully performed SID on mobility-selected protein complexes, including the streptavidin tetramer and cholera toxin B with bound ligands. Additionally, TIMS-SID was employed on a mixture of the peptides desArg1 and desArg9 bradykinin to mobility-separate and identify the individual peptides. Importantly, results show that </description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Apr</publication><modification>2025-04-05T14:05:38.422Z</modification><creation>2025-04-05T14:05:38.422Z</creation></dates><accession>S-EPMC8168055</accession><cross_references><pubmed>33751887</pubmed><doi>10.1021/acs.analchem.0c05373</doi></cross_references></HashMap>