Questions: A high fever causes an enzyme to lose its three-dimensional structure and function. Which bonds are broken when a protein denatures? hydrogen bonds non-polar covalent bonds ionic bonds polar covalent bonds

The answer is the first one: hydrogen bonds.

Explanation for each option:

• Hydrogen bonds: These are weak bonds that help maintain the three-dimensional structure of proteins. When a protein denatures due to high fever or other factors, these bonds are often disrupted, leading to the loss of the protein's structure and function.

• Non-polar covalent bonds: These bonds are strong and typically not broken during denaturation. They are responsible for the primary structure of the protein, which remains intact even when the protein denatures.

• Ionic bonds: While ionic bonds can be affected by changes in pH or ionic strength, they are not the primary bonds broken during thermal denaturation. However, they can contribute to the overall stability of the protein's structure.

• Polar covalent bonds: These bonds are also strong and are not typically broken during denaturation. They are involved in the primary structure of the protein.

In summary, when a protein denatures due to high fever, it is primarily the hydrogen bonds that are broken, leading to the loss of its three-dimensional structure and function.