Cystinuria is a metabolic disease that occurs in some breeds...

Cystinuria is a metabolic disease that occurs in some breeds of dogs. It is characterized by the presence of kidney stones made of cystine, a dimer formed when two cysteine residues covalently link through an $-\mathrm{S}-\mathrm{S}$ - bond (Figure 20.27 ). a. Draw the structure of the dipeptide Cys-Cys. b. Is cystine a dipeptide? Why or why not? (FIGURE CAN'T COPY)

Cystinuria is a metabolic disease that occurs in some breeds of dogs. It is characterized by the presence of kidney stones made of cystine, a dimer formed when two cysteine residues covalently link through an $-\mathrm{S}-\mathrm{S}$ - bond (Figure 20.27 ).
a. Draw the structure of the dipeptide Cys-Cys.
b. Is cystine a dipeptide? Why or why not?

(FIGURE CAN'T COPY)

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Key Concepts

Disulfide Bond

A disulfide bond is a covalent bond formed between the thiol groups of two cysteine residues. Unlike peptide bonds, these S-S bonds create linkages that stabilize the three-dimensional structure of proteins or result in dimerization of certain amino acids, such as linking two cysteine molecules to form cystine.

Amino Acids

Amino acids are the building blocks of proteins, each consisting of an amino group, a carboxyl group, and a unique side chain. Their structures determine how they interact and form larger molecules. Understanding the functional groups of amino acids is crucial in predicting how they bond together or participate in additional linking reactions.

Peptide Bond

A peptide bond is an amide linkage formed through a condensation reaction between the carboxyl group of one amino acid and the amino group of another. This bond is the primary connection within peptides and proteins, and it leads to the formation of dipeptides, tripeptides, and larger polypeptides.

Dipeptide

A dipeptide is a molecule composed of two amino acids connected by a single peptide bond. It represents the simplest form of a peptide, and its structure specifically involves the formation of an amide bond, rather than any additional types of covalent bonding.

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