Test: MCAT Biology

Proteins can have a maximum of four levels of structure: primary, secondary, tertiary, and quaternary. Although the proteins can spontaneously fold to a functional conformation, there are a variety of denaturing agents that can be used to disrupt the folding strategies of proteins. Mercaptoethanol is an example of a protein denaturing agent; its mechanism for dismantling proteins is to disrupt the disulfide bonds found in the protein. When urea is introduced to a protein, the hydrogen bonds holding the protein together are disrupted. Heat can also be considered a denaturing agent, which has the potential to disrupt all intermolecular interactions in a protein.

6.

Which of the following proteins would be least affected by the introduction of mercaptoethanol?

A protein that has no cysteine amino acid residues

A protein with no proline amino acid residues

A protein with no quaternary structure

A protein that can not form alpha-helices

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