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Your submitted paragraph: Post-translational modification of proteins TEXTBOOKS represent proteins chemically as a series of amino acid residues linked by peptide bonds and, in discussing protein biosynthesis, they emphasize the process by which such a linear polypeptide is assembled (see PROTEIN STRUCTURE; PROTEIN SYNTHESIS). But in most cases, the formation of a functional protein requires chemical events distinct from, and subsequent to, the sequential construction of the POLYPEPTIDE CHAIN. Such chemical processes are described as post- translational modifications [1-7]. They may be modifications which introduce new functional groups into a protein, providing it with a chemical property absent from the side chains of the 20 genetically encoded amino acids. Or they may be reversible modifications which act to switch a protein between two distinct functional states. They may be modifications of the N-terminal free amino group, or of specific side chains, or even specific proteolytic cleavage of the polypeptide representing the genetically encoded translation product. They may be the products of specific enzyme activity, or arise from non-enzymatic processes. They may occur so early in the life of an individual protein molecule as to be more properly described as co- translational, rather than post- translational modifications, or they may mark late events leading to the protein's final degradation and turnover (see PROTEIN DEGRADATION). They may take place in the cytoplasm, or in a subsequent subcellular compartment, or extracellularly. It is clearly possible to classify and discuss post-translational modifications in terms of any one of these distinctions. The comprehensive listings in [1,2] use a classification by residue modified. Post-translational modifications will be discussed here in terms of their location in the cell and their place in a protein's `life history'.

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