The description that matches the folding of soluble globular proteins is that hydrophobic amino acids are internal, while hydrophilic residues are on the surface, to stabilize protein structure in an aqueous environment. Option d is the correct option.
The folding of soluble globular proteins involves the interior positioning of hydrophobic amino acids, away from the surrounding water, while the hydrophilic amino acids are typically found on the exterior surface of the protein that interacts with the aqueous environment. This orientation of amino acids reduces the overall energy of the system and stabilizes the protein structure through the formation of various types of non-covalent interactions such as hydrogen bonds, van der Waals forces, ionic interactions, and hydrophobic interactions. Moreover, cysteine side chains can form covalent disulfide bonds which contribute to the folding and stability of the protein.
Folding ensures that globular proteins achieve their functional three-dimensional shape, which is critical for their biological activity. Incorrect folding can result in loss of function and diseases. Therefore, the correct choice describing the folding of soluble globular proteins is that most hydrophobic amino acids are internal, away from solvent water. Option d is the correct option.
The appropriate question is:
which of the following describes the folding of soluble globular proteins? group of answer choices
a) the energy of the system (protein water) is at a maximum
b) most hydrophilic amino acid residues are protected from aqueous environment
c) most peptide bonds are positioned outward towards water
d) most hydrophobic amino acids are internal, away from solvent water