Final answer:
It is false that an enzyme without disulfide linkages will be totally denatured in a urea solution; denaturation depends on several factors and interactions, not only disulfide bonds.
Step-by-step explanation:
It is false that an enzyme placed in a solution containing urea and having no disulfide linkages will be totally denatured by the treatment.
Enzymes are proteins with specific three-dimensional structures essential for their function. These structures can be disrupted by factors such as changes in temperature, pH, or exposure to certain chemicals, leading to a process known as denaturation. Denaturation affects the secondary through quaternary structures without breaking the peptide bonds of the primary structure. However, it is not solely dependent on the presence of disulfide linkages but also on other stabilizing interactions like hydrogen bonding and ionic bonds. The delicately folded proteins are more susceptible to denaturation compared to fibrous proteins. It is crucial to consider that not all denaturation is irreversible, and some proteins can refold and regain their function once the denaturing agent is removed.