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Nmr-Based Structural Studies Of The Glycosylated Muc1 Tandem Repeat Peptide, G. Suryanarayanan, P. A. Keifer, G. Wang, L. Kinarsky, M. A. Hollingsworth, S. Sherman
Nmr-Based Structural Studies Of The Glycosylated Muc1 Tandem Repeat Peptide, G. Suryanarayanan, P. A. Keifer, G. Wang, L. Kinarsky, M. A. Hollingsworth, S. Sherman
Journal Articles: Eppley Institute
MUC1 is a glycoprotein that plays an important role in cancer pathogenesis. In order to study the effect of glycosylation on the conformational propensities of the tandem repeat domain of MUC1, we have determined the structure of the MUC1 tandem repeat peptide AHGVTSAPDTRPAPGSTAPP, O-glycosylated with the trisaccharide (α-Glc-1,4-β-Glc-1,4-α-GalNAc-) at Thr5. This glycopeptide was synthesized to model a heavily Oglycosylated threonine residue in the tandem repeat domain. The NMR experiments used in this study included TOCSY, NOESY, ROESY, DQF-COSY, HSQC and 1D NMR. The peak volumes determined using the program SPARKY were converted into distance constraints using the program CALIBA. The …