Final answer:
A globular protein is characterized by a hydrophobic core and stabilized by the hydrophobic effect confirming that answer a) Hydrophobic; hydrophobic is correct. This structure helps protect the hydrophobic amino acids from water, while allowing hydrophilic amino acids to interact with the aqueous environment.
Step-by-step explanation:
A globular protein has a hydrophobic core and is stabilized primarily by the hydrophobic effect. Therefore, the correct answer is a) Hydrophobic; hydrophobic. In globular proteins, the polypeptide chain folds in such a way that the hydrophobic amino acids are shielded from the aqueous environment by being placed on the inside, while the hydrophilic amino acids are on the surface of the molecule where they can interact with water. This folding pattern contributes to the protein's stability along with other interactions such as ionic bonding, hydrogen bonding, disulfide linkages, and dispersion forces (Van der Waals forces).
The hydrophobic core helps to stabilize the protein's three-dimensional structure, as nonpolar amino acids lay in the interior, and the hydrophilic R groups face outwards. Interactions between cysteine side chains can form disulfide linkages, which are covalent bonds that further support protein folding and stability.