Characterization of an Eleven Residue MUC-1 Peptide Structure in Solution by 2D NMR Sprectroscopy

dc.contributor.advisor	Yang, Thao
dc.contributor.author	McAnally, Michael
dc.date.accessioned	2010-11-10T18:34:35Z
dc.date.available	2010-11-10T18:34:35Z
dc.date.issued	2010-04
dc.description	Color poster with text and images.	en
dc.description.abstract	MUC-1 peptides are peptides based on the amino acid sequence of the tandem repeat domain of mucin expressed by cancer cells, which immunity in a host could be induced against. MUC-1 peptides have been used as antigenic agents in the development of cancer vaccine. The purpose of this research is to better understand the specific conformation of a specific MUC-1 peptide. To address the question, we have synthesized an 11-mer peptide with the sequence GVTSAPDTRPA that spans the main portion of the tandem repeat domain of mucin that is known to bind to MUC-1 monoclonal antibody.	en
dc.description.sponsorship	University of Wisconsin--Eau Claire Office of Research and Sponsored Programs; Ronald E. McNair Postbaccalaureate Achievement Program	en
dc.identifier.uri	http://digital.library.wisc.edu/1793/47200
dc.language.iso	en_US	en
dc.relation.ispartofseries	USGZE AS589	en
dc.subject	MUC-1 peptides	en
dc.subject	Nuclear magnetic resonance spectroscopy	en
dc.subject	Peptides--Spectra	en
dc.subject	Posters	en
dc.title	Characterization of an Eleven Residue MUC-1 Peptide Structure in Solution by 2D NMR Sprectroscopy	en
dc.type	Presentation	en

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