Question

The tertiary structure of a given protein contains an interaction between aspartic acid and lysine.

A. Explain how the structure of amino acids determine the function.

Answer 1

The tertiary structure of a protein is determined by various chemical interactions, including ionic bonding, hydrogen bonding, and disulfide linkages. These interactions are formed between different amino acids and play a crucial role in determining the function of the protein.

Step-by-step explanation:

The function of a protein is determined by its structure, including the tertiary structure. In the tertiary structure, there can be interactions between different amino acids, such as aspartic acid and lysine. These interactions are formed through various chemical forces, such as ionic bonding, hydrogen bonding, and disulfide linkages.

Ionic bonding occurs when there is an attraction between positively and negatively charged side chains of amino acids. For example, the aspartic acid carboxylate ion is attracted to the lysine ammonium ion.

Hydrogen bonding forms between specific atoms in the amino acid side chains, such as electronegative oxygen or nitrogen atoms and hydrogen atoms attached to other oxygen or nitrogen atoms. This type of bonding is important for both intra- and intermolecular interactions in proteins.

Disulfide linkages occur when two cysteine amino acid units are brought close together and the sulfur atoms in their sulfhydryl groups oxidize and link. These linkages help stabilize the three-dimensional structure of the protein.

Answer 2

Amino acids determine the protein's function by affecting its folding and tertiary structure, which is stabilized by interactions like ionic bonding between aspartic acid and lysine, essential for biological activity.

Step-by-step explanation:

The structure of amino acids plays a crucial role in determining the function of proteins because it affects how the protein folds into its unique three-dimensional shape, known as its tertiary structure. The tertiary structure is stabilized by various chemical interactions, including ionic bonding, hydrogen bonding, hydrophobic interactions, and disulfide linkages. For example, the interaction between the negatively charged carboxylate ion of aspartic acid and the positively charged ammonium ion of lysine results in an ionic bond. This type of bond is critical for maintaining the protein's structure and, consequently, its function. These interactions are essential for the protein to achieve its final folded form, which is necessary for its specific biological activity.