<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Qu Y</submitter><funding>DOE-BER</funding><funding>EMSL intramural research projects</funding><funding>EMSL capability development projects</funding><funding>NIEHS NIH HHS</funding><funding>National Institute of Environmental Health Sciences of the National Institutes of Health</funding><funding>U.S. Department of Energy Office of Biological and Environmental Research</funding><funding>DOE</funding><pagination>207-215</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5175459</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>72</volume><pubmed_abstract>Protein glycosylation, an important and complex post-translational modification (PTM), is involved in various biological processes, including the receptor-ligand and cell-cell interaction, and plays a crucial role in many biological functions. However, little is known about the glycan structures of important biological complex samples, and the conventional glycan enrichment strategy (i.e., size-exclusion column [SEC] separation) prior to nuclear magnetic resonance (NMR) detection is time-consuming and tedious. In this study, we developed a glycan enrichment strategy that couples Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) with dialysis to enrich the glycans from the pronase E digests of RNase B, followed by NMR analysis of the glycoconjugate. Our results suggest </pubmed_abstract><journal>Fungal genetics and biology : FG &amp; B</journal><pubmed_title>Structural analysis of N- and O-glycans using ZIC-HILIC/dialysis coupled to NMR detection.</pubmed_title><pmcid>PMC5175459</pmcid><funding_grant_id>R01ES022176</funding_grant_id><funding_grant_id>R01 ES022176</funding_grant_id><funding_grant_id>DE-AC05-76RL01830</funding_grant_id><pubmed_authors>Cao L</pubmed_authors><pubmed_authors>Zink EM</pubmed_authors><pubmed_authors>Deng S</pubmed_authors><pubmed_authors>Lipton MS</pubmed_authors><pubmed_authors>Pasa-Tolic L</pubmed_authors><pubmed_authors>Zhang Q</pubmed_authors><pubmed_authors>Hu JZ</pubmed_authors><pubmed_authors>Jiang Y</pubmed_authors><pubmed_authors>Feng J</pubmed_authors><pubmed_authors>Zhao R</pubmed_authors><pubmed_authors>Zhang Z</pubmed_authors><pubmed_authors>Wu S</pubmed_authors><pubmed_authors>Qu Y</pubmed_authors><pubmed_authors>Baker SE</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural analysis of N- and O-glycans using ZIC-HILIC/dialysis coupled to NMR detection.</name><description>Protein glycosylation, an important and complex post-translational modification (PTM), is involved in various biological processes, including the receptor-ligand and cell-cell interaction, and plays a crucial role in many biological functions. However, little is known about the glycan structures of important biological complex samples, and the conventional glycan enrichment strategy (i.e., size-exclusion column [SEC] separation) prior to nuclear magnetic resonance (NMR) detection is time-consuming and tedious. In this study, we developed a glycan enrichment strategy that couples Zwitterionic hydrophilic interaction liquid chromatography (ZIC-HILIC) with dialysis to enrich the glycans from the pronase E digests of RNase B, followed by NMR analysis of the glycoconjugate. Our results suggest </description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Nov</publication><modification>2025-04-18T23:59:20.908Z</modification><creation>2019-03-27T02:32:12Z</creation></dates><accession>S-EPMC5175459</accession><cross_references><pubmed>25117693</pubmed><doi>10.1016/j.fgb.2014.08.001</doi></cross_references></HashMap>