Carbon is a ubiquitous element in all organic entities. Its presence in various biomolecules is of importance with regards to their structure and function. For amino acids, carbon is the only element which contributes to their hydrophobicity. Proteins necessitate presence of 31.44% carbon and approximately 27% large hydrophobic residues for structural stability. The structural accuracy of proteins is determined by hydrophobicity of its constituent residues. Similarly, post translational events also affect structural and functional aspects of proteins. Glycosylation is a universal post translational modification. It is known to influence protein folding, stability/turnover, solubility, sub-cellular localization and recognition events. Carbon being the sole contributor towards hydrophobicity, its presence is vital towards the precision of the protein function. Understanding this conception with profound study, may lead to a new dimension of protein sequence analysis. In this research we have analyzed presence and distribution of carbon percentage in and around sites of glycosylation in eukaryotic proteins. The study revealed that the site of glycosylation was flanked by sites possessing steep rise and steep dip in carbon percentage. So we may mark potential site of glycosylation by observing steep rise or dip in carbon percentage of the sequence. The site of glycosylation was seen to achieve a mean carbon percentage which was nearing mean carbon percentage for the total sequence. Thus, it was also observed that amount of carbon was being stabilized at the site of glycosylation.