Question

Globular proteins are stabilized by ______ forces and are easily unfolded or denatured by (list 4):

a) Covalent; heat, pH changes, chaotropic agents, reducing agents
b) Hydrophobic; pH changes, heat, ionic strength, denaturing agents
c) Hydrogen bonding; heat, chaotropic agents, pH changes, reducing agents
d) Van der Waals; heat, reducing agents, ionic strength, denaturing agents

Answer 1

Globular proteins are stabilized by hydrophobic forces and can be easily denatured by pH changes, heat, ionic strength, and denaturing agents.

Step-by-step explanation:

Globular proteins are stabilized by a variety of interactions, including hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide linkages. These delicate structures can be denatured through a range of agents and conditions. The answer to the question of what forces stabilize globular proteins and what can lead to their denaturation or unfolding is option (b) Hydrophobic forces; and they can be unfolded by pH changes, heat, ionic strength, and denaturing agents.

At the secondary through quaternary levels of protein structure, these proteins are vulnerable to denaturation, which can occur via different mechanisms such as changes in heat, pH, ionic strength, and the presence of denaturing agents. This denaturation process represents the unfolding of proteins into almost linear polypeptide chains, causing them to lose their functionality.