{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Duerr V"],"funding":["Waters Corporation through iCASE partnership PhD programmes","Medical Research Centre","European Commission","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["e70168"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12102732"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(6)"],"pubmed_abstract":["Hydrogen/deuterium exchange-mass spectrometry (HDX-MS) is a powerful tool for studying protein structure and dynamics. As a bottom-up LC-MS technique, its success largely depends on peptide identifications made by peptide mapping prior to HDX measurements. We previously demonstrated that combining peptide mapping results from complementary single- and multipass cyclic ion mobility-mass spectrometry (cIM-MS) experiments, an approach we term \"multi-sequence\" cIM-MS, can enhance HDX-MS by increasing peptide identifications. However, this approach required labor-intensive, manual handling of the acquired data, including lengthy optimization of drift time (DT) versus DT full width half maximum (FWHM) trendlines during peak detection processing to combat cyclic wrap-around effects. Here, we pres"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS."],"pmcid":["PMC12102732"],"funding_grant_id":["101183630","MR/X013030/1","EP/V011715/1","BB/V006487/2","BB/Y004981/1"],"pubmed_authors":["Politis A","Duerr V","Griffiths D"],"additional_accession":[]},"is_claimable":false,"name":"MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS.","description":"Hydrogen/deuterium exchange-mass spectrometry (HDX-MS) is a powerful tool for studying protein structure and dynamics. As a bottom-up LC-MS technique, its success largely depends on peptide identifications made by peptide mapping prior to HDX measurements. We previously demonstrated that combining peptide mapping results from complementary single- and multipass cyclic ion mobility-mass spectrometry (cIM-MS) experiments, an approach we term \"multi-sequence\" cIM-MS, can enhance HDX-MS by increasing peptide identifications. However, this approach required labor-intensive, manual handling of the acquired data, including lengthy optimization of drift time (DT) versus DT full width half maximum (FWHM) trendlines during peak detection processing to combat cyclic wrap-around effects. Here, we pres","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jun","modification":"2026-06-01T11:36:48.496Z","creation":"2026-04-08T11:56:45.722Z"},"accession":"S-EPMC12102732","cross_references":{"pubmed":["40411377"],"doi":["10.1002/pro.70168"]}}