Structural Properties of Substituted Mucin Peptides in Solution by 2D NMR
| dc.contributor.advisor | Yang, Thao | |
| dc.contributor.author | Her, Cheng | |
| dc.date.accessioned | 2011-11-11T20:43:22Z | |
| dc.date.available | 2011-11-11T20:43:22Z | |
| dc.date.issued | 2011-05 | |
| dc.description | Color poster with text, images, and charts. | en |
| dc.description.abstract | The 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.sponsorship | University of Wisconsin--Eau Claire Office of Research and Sponsored Programs | en |
| dc.identifier.uri | http://digital.library.wisc.edu/1793/55107 | |
| dc.language.iso | en_US | en |
| dc.relation.ispartofseries | USGZE AS589 | en |
| dc.subject | Mucins--Analysis | en |
| dc.subject | Peptides--Analysis | en |
| dc.subject | Nuclear magnetic resonance | en |
| dc.subject | Posters | en |
| dc.subject | Monoclanal antibodies | en |
| dc.title | Structural Properties of Substituted Mucin Peptides in Solution by 2D NMR | en |
| dc.type | Presentation | en |