Tag: Protein modification

Over 90% of protein oxidation occurs on specific amino acid residues, fundamentally altering protein structure and function. Understanding which amino acids can undergo oxidation is vital for investigating cellular damage, aging, and the mechanisms underlying various diseases. This process affects not only individual proteins but can also play a crucial role in overall cellular signaling and metabolic health.

Collagen, the most abundant protein in the body, owes its remarkable tensile strength and unique structure to a special modification: the addition of hydroxyproline. This process, which occurs after initial synthesis, is fundamentally important for producing stable collagen fibers that form the structural framework of skin, bones, and cartilage.

As one of the nine essential amino acids, lysine plays a remarkably versatile and vital role in protein function and structure. The function of lysine in proteins ranges from providing structural stability through charge interactions to acting as a site for crucial regulatory modifications.

Myristic acid, a 14-carbon saturated fatty acid, constitutes approximately 1% of all endogenous fatty acids in the human body, but its influence on cellular processes is disproportionately significant. Primarily known for its role in protein modification, this compound is a crucial component for cell signaling pathways, structural integrity, and immune system functions.