{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":48,"searchCount":0},"additional":{"submitter":["Seo Y"],"funding":["NIGMS NIH HHS"],"pagination":["191-198"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3124288"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["303(2-3)"],"pubmed_abstract":["Heparin interacts with many proteins and is involved in biological processes such as anticoagulation, angiogenesis, and antitumorigenic activities. These heparin-protein interactions can be influenced by the binding of various metal ions to these complexes. In particular, physiologically relevant metal cations influence heparin-protein conformations through electronic interactions inherent to this polyanion. In this study, we employed ion mobility mass spectrometry (IMMS) to observe conformational changes that occur in fully-sulfated heparin octasaccharides after the successive addition of metal ions. Our results indicate that binding of positive counter ions causes a decrease in collision cross section (CCS) measurements, thus promoting a more compact octasaccharide structure."],"journal":["International journal of mass spectrometry"],"pubmed_title":["Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry."],"pmcid":["PMC3124288"],"funding_grant_id":["R01 GM047356","R01 GM047356-19"],"pubmed_authors":["Schenauer MR","Seo Y","Leary JA"],"view_count":["48"],"additional_accession":[]},"is_claimable":false,"name":"Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry.","description":"Heparin interacts with many proteins and is involved in biological processes such as anticoagulation, angiogenesis, and antitumorigenic activities. These heparin-protein interactions can be influenced by the binding of various metal ions to these complexes. In particular, physiologically relevant metal cations influence heparin-protein conformations through electronic interactions inherent to this polyanion. In this study, we employed ion mobility mass spectrometry (IMMS) to observe conformational changes that occur in fully-sulfated heparin octasaccharides after the successive addition of metal ions. Our results indicate that binding of positive counter ions causes a decrease in collision cross section (CCS) measurements, thus promoting a more compact octasaccharide structure.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2024-11-15T08:32:22.612Z","creation":"2019-03-27T00:43:03Z"},"accession":"S-EPMC3124288","cross_references":{"pubmed":["21731426"],"doi":["10.1016/j.ijms.2011.02.003"]}}