<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>48</viewCount><searchCount>0</searchCount></scores><additional><submitter>Seo Y</submitter><funding>NIGMS NIH HHS</funding><pagination>191-198</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3124288</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>303(2-3)</volume><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.</pubmed_abstract><journal>International journal of mass spectrometry</journal><pubmed_title>Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry.</pubmed_title><pmcid>PMC3124288</pmcid><funding_grant_id>R01 GM047356</funding_grant_id><funding_grant_id>R01 GM047356-19</funding_grant_id><pubmed_authors>Schenauer MR</pubmed_authors><pubmed_authors>Seo Y</pubmed_authors><pubmed_authors>Leary JA</pubmed_authors><view_count>48</view_count></additional><is_claimable>false</is_claimable><name>Biologically Relevant Metal-Cation Binding Induces Conformational Changes in Heparin Oligosaccharides as Measured by Ion Mobility Mass Spectrometry.</name><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.</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Jun</publication><modification>2024-11-15T08:32:22.612Z</modification><creation>2019-03-27T00:43:03Z</creation></dates><accession>S-EPMC3124288</accession><cross_references><pubmed>21731426</pubmed><doi>10.1016/j.ijms.2011.02.003</doi></cross_references></HashMap>