PEPTIDES & PROTEINS
Peptides and proteins are amino acid polymers in which the individual amino acids, called residues, are joined together by amide bonds, or peptide bonds. An amino group from one residue forms an amide bond with the carboxyl of a second residue, the amino group of the second forms an amide bond with the carboxyl of a third, and so on. For example, alanylserine is the dipeptide that results when an amide bond forms between the alanine carboxyl and the serine amino group:
Note that two dipeptides can result from reaction between alanine and serine, depending on which carboxyl group reacts with which amino group. If the alanine amino group reacts with the serine carboxyl, serylalanine results:
The long, repetitive sequence of –N–CH–CO– atoms that makes up a continuous chain is called the protein’s backbone. By convention, peptides are
written with the N-terminal amino acid (the one with the free –NH3 group) on the left and the C-terminal amino acid (the one with the free –CO2 group)
on the right. Thus, alanylserine is abbreviated Ala-Ser or A-S, and serylalanine is abbreviated Ser-Ala or S-A. Needless to say, the one-letter abbreviations are more convenient than the older three-letter abbreviations.
The amide bond that links different amino acids together in peptides is no different from any other amide bond. An amide nitrogen is nonbasic because its unshared electron pair is delocalized by interaction with the carbonyl group. This overlap of the nitrogen p orbital with the p orbitals of the carbonyl group imparts a certain amount of double-bond character to the C–N bond and restricts rotation around it. The amide bond is therefore planar, and the N–H is oriented 180° to the C=O.
written with the N-terminal amino acid (the one with the free –NH3 group) on the left and the C-terminal amino acid (the one with the free –CO2 group)
on the right. Thus, alanylserine is abbreviated Ala-Ser or A-S, and serylalanine is abbreviated Ser-Ala or S-A. Needless to say, the one-letter abbreviations are more convenient than the older three-letter abbreviations.
The amide bond that links different amino acids together in peptides is no different from any other amide bond. An amide nitrogen is nonbasic because its unshared electron pair is delocalized by interaction with the carbonyl group. This overlap of the nitrogen p orbital with the p orbitals of the carbonyl group imparts a certain amount of double-bond character to the C–N bond and restricts rotation around it. The amide bond is therefore planar, and the N–H is oriented 180° to the C=O.
A second kind of covalent bonding in peptides occurs when a disulfide linkage, RS–SR, is formed between two cysteine residues. A disulfide is formed by mild oxidation of a thiol, RSH, and is cleaved by mild reduction.
A disulfide bond between cysteine residues in different peptide chains links the otherwise separate chains together, while a disulfide bond between cysteine residues in the same chain forms a loop. Such is the case, for instance, with vasopressin, an antidiuretic hormone found in the pituitary gland. Note that the C-terminal end of vasopressin occurs as the primary amide, –CONH2, rather than as the free acid.