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AP Bio Final Rev Biochem

Total questions: 20

Worksheet time: 29mins

Name
Class
Date
1.

Which of the following is most closely related to the secondary structure of proteins?

a)

lipids

b)

peptide bonds

c)

alpha helix

d)

cellulose

2.

Which two functional groups are always found in amino acids?

a)

amine and sulfhydryl

b)

hydroxyl and carboxyl

c)

carboxyl and amine

d)

phosphate group and nitrogenous base

3.

The tremendous variation and unique properties of proteins are most likely a result of

a)

interactions between R groups of the amino acids

b)

hydrogen bonds lining amino acids

c)

the sequence of amino acids in the primary structure of the protein

d)

peptide bonds lining amino and carboxyl groups

4.

Water is an excellent solvent. Select the property that justifies this statement.

a)

as a polar molecule, it can surround and dissolve ionic and polar molecules

b)

it forms ionic bonds with ions, hydrogen bonds with polar molecules, and hydrophobic interactions with non polar molecules

c)

it forms hydrogen bonds with itself so cohesion is possible

d)

it is liquid and will adhere to many substances

5.

which is a protein monomer?

a)
b)
c)
d)
6.
What type of macromolecule is shown in the image below?
a)
Carbohydrate
b)
Nucleic Acid
c)
Fatty Acid
d)
Protein
7.
An unknown molecule contains a sugar and a phosphate group. It is likely what?
a)
carbohydrate
b)
protein
c)
lipid
d)
nucleic acid
8.
Identify the macromolecule in the image below.
a)
carbohydrate
b)
nucleic acid
c)
protein
d)
lipid
9.

This image is of what type of macromolecule?

a)

lipid

b)

carbohydrate

c)

protein

d)

nucleic acid

10.

The partial negative charge at one end of a water molecule is attracted to a partial positive charge of another water molecule. What is this type of attraction called?

a)

a polar covalent bond

b)

an ionic bond

c)

a hydration shell

d)

a hydrogen bond

11.

The diagram shows a bond forming between two amino acids. What is the name of this reaction?

a)

Dehydration Synthesis

b)

Hydrolysis

c)

Pepysis

d)

Oxidation

12.
Why does ice float?
a)
As water freezes, it expands and its density decreases.
b)
As water freezes, it takes up more hydrogen from the atmosphere, causing it to have a greater buoyancy.
c)
As water freezes, air becomes trapped between the hydrogen bonds of water molecules.
d)
As water freezes, it takes up more oxygen from the atmosphere, causing it to have a greater buoyancy.
13.

How might an amino acid change at a site distant from the active site of the enzyme alter the enzyme's substrate specificity?

a)

by changing the enzyme's stability

b)

by changing the enzyme's location in the cell

c)

by changing the shape of the protein

d)

by changing the enzyme's pH optimum

14.

For the enzyme-catalyzed reaction shown in Figure 6.2, which of these treatments will cause the greatest increase in the rate of the reaction, if the initial reactant concentration is 1.0 micromolar?

a)

doubling the activation energy needed

b)

cooling the reaction by 10°C

c)

doubling the concentration of the reactants to 2.0 micromolar

d)

doubling the enzyme concentration

15.

In Figure 6.2, why does the reaction rate plateau at higher reactant concentrations?

a)

Feedback inhibition by product occurs at high reactant concentrations.

b)

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

c)

The reaction nears equilibrium at high reactant concentrations.

d)

The activation energy for the reaction increases with reactant concentration.

16.

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

a)

a

b)

b

c)

c

d)

d

17.
Succinate dehydrogenase catalyzes the conversion of succinate to fumarate. The reaction is inhibited by malonic acid, which resembles succinate but cannot be acted upon by succinate dehydrogenase. Increasing the ratio of succinate to malonic acid reduces the inhibitory effect of malonic acid. What is malonic acid's role with respect to succinate dehydrogenase?
a)
It is a competitive inhibitor.
b)
It is an allosteric regulator.
c)
It is able to bind to succinate.
d)
It blocks the binding of fumarate.
18.

Fireflies emit light. The production of light by an organism is called bioluminescence. To generate visible light, cells in a firefly’s tail produce thousands of luciferase enzymes. Luciferase binds to a chemical called luciferin. Once bound, the luciferase enzyme speeds up a chemical reaction that combines an oxygen molecule and luciferin to produce oxyluciferin. This reaction requires energy and releases light. Which of the following best describes how the luciferase enzyme speeds up the chemical reaction?

a)

Luciferase increases the amount of time the light is visible.

b)

Luciferase decreases the amount of energy required for the reaction to start.

c)

Luciferase increases the number of sites on luciferin that must bind to oxygen.

d)

Luciferase decreases the temperature of the environment inside the body of the firefly.

19.

Pepsin and trypsin are two of the digestive enzymes that break down protein. A group of students studied the pH requirements of these enzymes. The graph below shows the results.


The students found that pepsin functions best in an acid environment and trypsin functions best in a neutral environment. Based on their observations, pepsin most likely aids in digestion in which part of the human body?

a)

Pancreas

b)

Intestines

c)

Mouth

d)

Stomach

20.

If nerve gasses are inhaled, they will temporarily bind to an area on many enzymes that will change the shape of the enzyme. This prevents the enzymes from interacting with other substances and interferes in proper nervous system functioning resulting in death. The nerve gas is an example of a(n):

a)

Substrate

b)

Activation Inhibitor

c)

Production Inhibitor

d)

Competitive Inhibitor

e)

Non-competitive Inhibitor