{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Panczyk EM"],"funding":["National Institutes of Health","NIGMS NIH HHS","NIH HHS"],"pagination":["5513-5520"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8168055"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["93(13)"],"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 "],"journal":["Analytical chemistry"],"pubmed_title":["Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry."],"pmcid":["PMC8168055"],"funding_grant_id":["S10 OD018507","P41GM128577","P41 GM128577"],"pubmed_authors":["Wysocki VH","Snyder DT","Panczyk EM","Park MA","Ridgeway ME","Somogyi A"],"additional_accession":[]},"is_claimable":false,"name":"Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry.","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 ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2025-04-05T14:05:38.422Z","creation":"2025-04-05T14:05:38.422Z"},"accession":"S-EPMC8168055","cross_references":{"pubmed":["33751887"],"doi":["10.1021/acs.analchem.0c05373"]}}