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Research Abstracts Online
January 2008 - March 2009

University of Minnesota Twin Cities
College of Biological Sciences and Medical School
Department of Biochemistry, Molecular Biology, and Biophysics

PI: David H. Live

Structure and Dynamics of Mucin Glycoproteins

These researchers are working to determine the structural and dynamic properties of mucin motifs. These motifs, characterized by regions of highly O-glycosylated protein, can be found in secreted mucin glycoproteins, in mucin domains of integral membrane cell-surface glycoproteins, and as components of the glycoprotein complexes in connective tissue. They can function both as purely structural elements and in molecular recognition by virtue of their ability to display a variety of carbohydrate epitopes on the same protein core. These researchers have reported on the structure of a mucin glycopeptide that has offered new insights into the intramolecular interactions between sugar and peptide components that aid in understanding the conformational features displayed by mucins. A noteworthy aspect of the NMR experiments was strong evidence for a well-defined organization even for a short mucin segment based on a glycosylated pentapeptide STTAV from the cell surface protein CD43. The researchers are obtaining additional structural data as well as 13C NMR relaxation measurements and are performing molecular dynamics (MD) calculations and analyzing them to further understand the properties of mucins. They are also carrying out studies on the conformation of glycopeptides from the glycoprotein a-dystroglycan, important in the organization of muscle tissue. As these results provide one of the few examples with extensive experimental structural restraints, the MD calculations are serving to further refine the force-field parameters for studying such molecules.

Group Member

Andrew Borgert, Graduate Student