Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Medicine and Health Sciences
Molecular Dynamics Simulations Of The O-Glycosylated 21-Residue Muc1 Peptides, A. Rubinstein, L. Kinarsky, S. Sherman
Molecular Dynamics Simulations Of The O-Glycosylated 21-Residue Muc1 Peptides, A. Rubinstein, L. Kinarsky, S. Sherman
Journal Articles: Eppley Institute
The conformational propensities of the 21-residue peptide and its Oglycosylated analogs were studied by molecular dynamics (MD) simulations. This polypeptide motif comprises the tandem repeat of the human mucin (MUC1) protein core that is differently glycosylated in normal and cancer cells. To evaluate the structural effects of O-glycosylation on the polypeptide backbone, conformations of the nonglycosylated peptide and its glycosylated analogs were monitored during the 1 ns MD simulations. Radius gyration for whole peptide and its fragments, as well as root-mean-square-deviation between coordinate sets of the backbone atoms of starting structures and generated structures, were calculated. It was shown that …