Glycoproteins typically attach to which amino acid residues?

Glycoproteins are proteins that have carbohydrate groups attached to them, and this modification typically occurs at specific amino acid residues. The primary amino acids involved in glycosylation are serine, threonine, and asparagine.

Serine and threonine can have O-linked glycosylation, where the carbohydrate is attached to the hydroxyl (-OH) side chain of these amino acids. Asparagine is involved in N-linked glycosylation, where the carbohydrate is attached to the nitrogen (-NH2) side chain of asparagine. This specific attachment is crucial for the structure and function of glycoproteins, influencing their stability, localization, and biological activity.

Understanding the roles of these specific amino acids in glycoprotein synthesis underscores the significance of glycosylation in cellular processes and protein function.