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dc.contributor.advisorYang, Thao
dc.contributor.authorHer, Cheng
dc.date.accessioned2011-11-11T20:43:22Z
dc.date.available2011-11-11T20:43:22Z
dc.date.issued2011-05
dc.identifier.urihttp://digital.library.wisc.edu/1793/55107
dc.descriptionColor poster with text, images, and charts.en
dc.description.abstractThe short mucin peptide with the sequence Glycine-Valine-Threonine-Serine-Alanine-Proline-Aspartic acid has been shown to have significant interactions with a specific monoclonal antibody. Its proline residue appears to be required for the binding. To explore the function of proline further, the structures of three substituted mucin peptides were studied. Two-dimensional nuclear magnetic resonance (2D NMR) was employed to study the structures of these peptides in aqueous solution.en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programsen
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectMucins--Analysisen
dc.subjectPeptides--Analysisen
dc.subjectNuclear magnetic resonanceen
dc.subjectPostersen
dc.subjectMonoclanal antibodiesen
dc.titleStructural Properties of Substituted Mucin Peptides in Solution by 2D NMRen
dc.typePresentationen


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