BIO1010 Module 6: Macromolecules - Proteins and Enzymes

These flashcards cover key terms and concepts related to proteins and enzymes, as outlined in the reading guide for the BIO1010 course.

Denaturation

The process in which proteins lose their shape due to the disruption of non-covalent interactions, resulting in a loss of function.

Specificity

The ability of an enzyme to choose exact substrates from a group of similar chemical molecules.

Peptide bond

A covalent bond that links amino acids together in a protein, formed between the carboxyl group of one amino acid and the amino group of another.

Primary structure

The linear sequence of amino acids in a protein, which determines its unique characteristics.

Secondary structure

The localized folding of the polypeptide chain into structures such as alpha helices and beta sheets, stabilized by hydrogen bonds.

Tertiary structure

The overall three-dimensional shape of a polypeptide, determined by interactions among various side chains (R groups).

Quaternary structure

The arrangement of multiple polypeptide chains into a single functional protein complex.

Hydrogen bonds

Weak chemical bonds that help stabilize the secondary, tertiary, and quaternary structures of proteins.

Ionic bonds

Electrostatic attractions between charged side chains that contribute to protein stability.

Hydrophobic interactions

Interactions among nonpolar side chains that drive them away from water and contribute to protein folding.

Optimal temperature

The temperature at which an enzyme functions best, corresponding to its highest activity.

Optimal pH

The specific pH at which an enzyme exhibits maximum activity, affecting its shape and reactions.

Active site

The region of an enzyme where substrate molecules bind and undergo a chemical reaction.

Substrate

The specific reactant that an enzyme acts upon.

Product

The resulting substance(s) formed as a result of the enzyme-catalyzed reaction.