Glycosylation Site Prediction

Background: Glycosylation is one of the most complex post-translational modifications (PTMs) of proteins in eukaryotic cells. Glycosylation plays an important role in biological processes ranging from protein folding and subcellular localization, to ligand recognition and cell-cell interactions. Experimental identification of glycosylation sites is expensive and laborious. Hence, there is significant interest in the development of computational methods for reliable prediction of glycosylation sites from amino acid sequences.

The precise characterization of post translational modifications (PTMs) is important for the understanding of protein regulatory mechanisms and their role in disease. However, experimental studies on PTMs, especially with multifunctional proteins are difficult to follow and investigate. Bioinformatic tools are therefore helpful in predicting key protein modifications. To study the role A. M. Butt Á M. Hussain Á M. Idress

A highly regio-and diastereo-selective synthesis of halogenated C-vinyl glycosides has been achieved from glycals and unactivated aryl acetylenes in the presence of halogenated Lewis acids via a tandem glycosylation-halogenation reaction. The Lewis acid used served the dual purpose of activating the allylic acetoxy group of glycals and serving as halogen source for Markovnikov addition across the triple bond, which makes the process atom economic.