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This course provides a brief overview of the key methods used to obtain homogeneous glycoproteins and mimics of thereof.It first describes this type of large biomolecules called glycoproteins, their structure and their essential roles in diverse biological processes. It emphasizes the importance of homogeneously glycosylated proteins in glyco-biology studies, where precise and consistent glycoforms are crucial for understanding glycoprotein functions.The course covers various methods to access homogeneous glycoforms, beginning with total chemical synthesis and the engineering of glycosylation pathways. It then explores the direct enzymatic protein glycosylation and glycoprotein remodeling as key techniques used to manipulate glycoproteins.You will also learn about site-selective chemical strategies, that either make use of a cysteine-derived chemical handle or of an unnatural amino acid tag inserted in the protein backbone. The cysteine incorporation is achieved via site-directed mutagenesis whereas unnatural amino acids can be introduced using the sense or nonsense reassignment methods. These approaches expand the toolkit available for site-selective protein-glycan ligation strategies.The course concludes with a practical lab example, demonstrating the site-selective glycosylation of a protein, tying theory to real-world application.By the end, you will hopefully have a good understanding of both theoretical concepts and practical methods used in glycoprotein chemical biology.

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