Protein tertiary structures
A) require the formation of disulfide bonds in order to achieve their native state.
B) are always irreversibly destroyed by the addition of denaturants, such as urea and salts, even when the denaturants are subsequently removed.
C) are often disrupted by the either very low pH or very high pH values as a result of alterations in the ionization states of acidic or basic amino acids.
D) are generally poorly defined and cannot be determined experimentally.

Question

Quizplus · Accepted Answer

Extreme pH values can affect the ionization states of acidic or basic amino acids, which can disrupt the interactions that stabilize the tertiary structure of a protein. Disulfide bonds (A) help stabilize tertiary structures but are not always required. Denaturants (B) can disrupt the tertiary structure, but it is not always irreversible, and some proteins can refold after denaturant removal. Option D is incorrect as protein tertiary structures can be experimentally determined using techniques like X-ray crystallography or NMR spectroscopy.

Protein Tertiary Structures