AP Bio Protein and Enzymes Practice Quiz

If a protein has only amino acids that have non-polar (hydrophobic) side chains is placed in water it will

• fold in half so the side chains are exposed to water

• unfold and work more efficiently

• fold in on itself so the side chains are away from water

• none of these

The level of protein structure that results from hydrogen bonding (between amino and carboxyl groups) causing the protein to fold into α-helix and β-pleated sheets is known as

• primary structure

• secondary structure

• tertiary structure

• quaternary structure

When a protein unfolds, it becomes

• Denatured

• More functional

• Has more amino acids added

• A carbohydrate

The main bonding in the secondary structure of a protein is due to.....

• covalent bonding
• ionic bonding
• hydrogen bonding
• polar bonding

The tertiary structure folding in proteins is caused by interactions of....

• the 'R' groups or side chains

• the peptide bonds of the backbone

• the amino groups

• the beta-sheets

Which letter corresponds to an alpha helix?

• A
• B
• C
• D

Which letter corresponds to an beta sheet?

• A
• B
• C
• D

Increasing the substrate concentration in an enzymatic reaction could overcome which of the following?

• denaturation of the enzyme

• non-competitive inhibition

• competitive inhibition

• addition of more inhibitor

In Figure 6.2, why does the reaction rate reach a maximum and remain there at higher reactant (substrate) concentrations?

• The product of the reaction is broken down

• Most enzyme molecules are occupied by substrate at high reactant concentrations.

• The enzyme is denatured at high reactant concentrations.

• The activation energy for the reaction increases with reactant concentration.

Tags

NGSS.HS-PS1-5

Which of the following in Figure 6.4 would be the same in either an enzyme-catalyzed or a noncatalyzed reaction?

• a

• b

• c

• d

Tags

NGSS.HS-PS1-4