Glycosylation is a collection of complex cotranslational/posttranslational covalent modifications of lipids and proteins. These modifications are of great importance as they affect the function and structure of such complex molecules. Researching complex molecules is very demanding and often requires combination of different types of methods. One such group includes bioinformatic methods whose main goals are data analysis and simulations. As the number of research papers grows, the amount of data on these molecules grows as well which consequently requires better and faster tools for data analysis. This Master’s thesis was an attempt of developing such a tool to improve the ones already available for UniProt database. The developed tool was tested on a set of 592 annotated human plasma glycoproteins. Computer analysis of the aforementioned set yielded the insight that most of these proteins were smaller than 1000 amino acids with masses under 100 kDa. It has also showed that most of these glycoprotein structures are hydrophilic in nature and that by far the most common type of glycosylation is the N-glycosylation. Analysis of peptides acquried by computer trypsine digestion was conducted as well. It showed that most of such peptides are much smaller than their glycoprotein counterparts, mostly ranging in size under 10 kDa or 100 amino acids in length and are less hydrophilic than full glycoproteomic structures.