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Glycosylation is a recently identified post-translational modification of proteins in prokaryotes. A glycan moiety is attached enzymatically to a protein by the process of glycosylation. Glycosylation is known to influence biological properties like activity, solubility, folding, conformation, stability, half-life, and/or immunogenicity of different cellular proteins thereby modulating the structure/function of these proteins for a variety of cellular/extracellular functions in a living cell. Determination of glycosite(s) is one important aspect of glycoprotein characterization. The experimental characterization of glycosite(s) and the glycoproteins, however, could be difficult, technically demanding, and time-consuming owing to the labile nature of modification involved as well as lack of high-senstivity yet cost-effective methods for glycoprotein detection. Therefore, the computational algorithms/models to predict glycosites in protein sequences are very useful in complementing and facilitating such studies.
(Chauhan et al., 2012) GlycoPP: a webserver for prediction of N- and O-glycosites in prokaryotic protein sequences. PLoS One.