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The attachment of the sugar N-acetylglucosamine (GlcNAc) to proteins occurs after the protein is folded into its 3D shape. The GlcNAc is transferred to the surface of the protein by the enzyme O-GlcNAc transferase (OGTase). This process is called glycosylation. Glycosylation is a normal process in mammals, including humans. However, when it becomes hyperactivated, it leads to health problems, including type II diabetes. If we could identify the requirements for glycosylation, it is possible that a drug could be derived that could be used to mediate this interaction and so treat diseases such as diabetes. In this thesis, we propose a method which adapt RMSD algorithm to identify the structural features in the vicinity of serine or threonine residues, which are responsible for directing the enzyme to a particular position in the protein.