Many Proteins Undergo Chemical Modification of Amino Acid Residues

Nearly every protein in a cell is chemically modified after its synthesis on a ribosome. Such modifications, which may alter the activity, life span, or cellular location of proteins, entail the linkage of a chemical group to the free -NH2 or -COOH group at either end of a protein or to a reactive side-chain group in an internal residue. Although cells use the 20 amino acids shown in Figure 2-13 to synthesize proteins, analysis of cellular proteins reveals that they contain upward of 100 different amino acids. Chemical modifications after synthesis account for this difference.

Acetylation, the addition of an acetyl group (CH3CO) to the amino group of the N-terminal residue, is the most common form of chemical modification, affecting an estimated 80 percent of all proteins:

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