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dc.contributor.advisorYang, Thao
dc.contributor.authorYang, Chee
dc.contributor.authorRose, Daniel H.
dc.date.accessioned2008-02-04T17:43:51Z
dc.date.available2008-02-04T17:43:51Z
dc.date.issued2007-05-01T17:43:51Z
dc.identifier.urihttp://digital.library.wisc.edu/1793/23177
dc.descriptionColor poster with text, charts and graphs describing research conducted by Chee Yang and Daniel H. Rose advised by Thao Yang.en
dc.description.abstractThe amino acid sequence Arg-Gly-Asp or RGD is present on several extracellular matrix proteins and known to be a requirement for their binding to integrins, which are a class of cell receptor proteins on cell surface. Some of the well-studied extracellular matrix proteins included fibrinogen, fibronectin, vitronectin, collagen, and laminin, which contains the RGD sequence. Subsequent studies in this project will focus on the conformational structures of the RGD-peptides and their binding properties to integrins. We present here the methodology for the synthesis of two linear RGD peptides using the Solid Phase Peptide Synthesis Method and some preliminary NMR data.en
dc.description.sponsorshipUniversity of Wisconsin-Eau Claire Office of Research and Sponosored Programs.en
dc.format.extent1680896 bytes
dc.format.extent763720 bytes
dc.format.mimetypeapplication/vnd.ms-powerpoint
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectIntegrinsen
dc.subjectAmino acidsen
dc.subjectPeptides--Synthesisen
dc.subjectPosters
dc.titleThe synthesis of RGD pepties via solid phase peptide synthesisen
dc.typePresentationen


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