1st SUMMATIVE ASSESSMENT

GENERAL BIOCHEMISTRY
MTY1109
INSTRUCTIONS:
 Choose the letter with the BEST answer.
 RATIONALIZED every choice in the choices of each question WHY IT IS THE
CORRECT/INCORRECT answer.
 5 points each item. TOTAL OF 100 POINTS

1. Which of the following is considered as structural polysaccharide?

A. Heparin C. Hyaluronic acid E. Glucose
B. Cellulose D. Starch

Explanation: They range in structure from linear to highly branched. Examples include

storage polysaccharides such as starch and glycogen, and structural polysaccharides such as
cellulose and chitin.

2. They are known as subtype of diastereomers whose molecules differ only in the
configuration at one chiral center.
A. Monomers C. Isomers E. None of the Above
B. Epimers D. All of the above

Explanation: the chiral center where each molecule differs is where their absolute
configuration is opposite that of the other pair.

3. Which of the following structures is that of an L-monosaccharide?

A. B. C. D.

4. What is the relationship between D-Galactose and L-Galactose?

A. Diastereomers C. Epimers E. Geometrical isomers
B. Enantiomers D. Cis-trans isomers

Explanation: So D-glucose and D-galactose are diastereomers. They have the same
connectivity but are different optical isomers that are not enantiomers.

5. Which of the following disaccharides has the same β (1 to 4) linkage.

A. Sucrose and Maltose
B. Maltose and Cellobiose
C. Mannose and Sucrose
D. Lactose and Cellobiose
E. Cellulose and Fructose

Explanation: Common Disaccharides. Sucrose, lactose, and maltose are

common dietary components. Lactose, the disaccharide of milk, consists of
galactose joined to glucose by a β-1,4-glycosidic linkage. Lactose is
hydrolyzed to these monosaccharides by lactase in human beings.

6. The only achiral amino acid.

A. Glu B. Gln C. Gly D. Glc E. Gle
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GENERAL BIOCHEMISTRY
MTY1109
Explanation: Glycine is the only amino acid with no asymmetric (chiral) carbon because it has two
hydrogens attached to alpha carbon.

7. Regeneration of the Carboxyl and Amino group of amino acids upon addition of water.
A. Protein Denaturation C. Protein Hydrolysis E. Protein Hydration
B. Peptide formation D. Peptide Hydrogenation

Explanation: A peptide bond is a chemical bond formed between two

molecules when the carboxyl group of one molecule reacts with the amino
group of the other molecule, releasing a molecule of water (H2O). This is a
dehydration synthesis reaction (also known as a condensation reaction), and
usually occurs between amino acids.
8. Which of the following statements about protein structure is correct?
A. The sequence of amino acids in a protein is its tertiary structure
B. The sequence of amino acids in a protein is its secondary structure
C. Cross-links formed by oxidation of -SH groups of cysteine to form disulfide bridges
render the amino acid unavailable to digestion.
D. Cross-links between the amino group of lysine and the carboxyl group of glutamate
render the amino acid(s) unavailable for digestion.
E. All proteins have the same secondary structure

Explanation: Tertiary structure is the next level of complexity in protein folding. Tertiary
structure is the three dimensional structure of a protein. While individual amino acids in
the primary sequence can interact with one another to form secondary structures such
as helices and sheets and individual amino acids from distant parts of the primary
sequence can intermingle via charge-charge, hydrophobic, disulfide, or other
interactions, the formation of these bonds and interactions, the formation of these bonds
and interactions will serve to change shape of the overall protein.

9. Statement 1: Insulin and Glucagon are transport proteins that regulates blood glucose.
Statement 2: Hemoglobin is classified as multimeric and has a tertiary structure.
A. Both statements are correct.
B. Both statements are incorrect.
C. 1st statement is correct; 2nd is incorrect.
D. 1st statement is incorrect; 2nd is correct.
Insulin helps cells absorb glucose, reducing blood sugar and providing the cells with
glucose for energy. When blood sugar levels are too low, the pancreas release glucagon
instructs the liver to release stored glucose, which causes blood sugar to rise.

10. Zwitterion form of Alanine:

A. B. C. D.

Explanation: An amino acid zwitterion arising from transfer of a proton from the carboxy to the
amino group of alanine; major species at pH 7.3.

11. Energy is primarily stored in the body in the form of ________.

A. Cholesterol C. Triglycerides E. Fatty acid salts
B. Lipoproteins D. Free fatty acids

Explanation: Triglycerides: The major form of fat stored by the body.

A triglyceride consists of three molecules of fatty acid combined with a
 1st SUMMATIVE ASSESSMENT
GENERAL BIOCHEMISTRY
MTY1109
molecule of the alcohol glycerol. Triglycerides serve as the backbone of
many types of lipids (fats). Triglycerides come from the food we eat as well
as from being produced by the body.

12. Which of the following is a characteristic of both triacylglycerols and

glycerophospholipids?
A. Both contain carboxyl groups and are amphipathic.
B. Both contain fatty acids and are saponifiable.
C. Both contain glycerol and ether bonds.
D. Both can be negatively charged at cellular pH.
E. Both contain one or more ester bonds.
The main constituents of membrane bilayers often called phospholipids, an imprecise
term, as other lipids contains phosphate.

13. Which of the following is true?

A. Polyunsaturated fatty acids tend to bend, causing less packing, thus making
them softer than their saturated counterparts.
B. A cis-monounsaturated fatty acid has the same 3D structure as their
unsaturated counterparts.
C. The more unsaturated a fatty acid is, the higher its melting point.
D. The melting point of fatty acids is not dependent on the number of carbons in
their chain.

Explanation: The geometry of the double bond is almost always a cis configuration in
natural fatty acids. These molecules do not "stack" very well. The intermolecular interactions are
much weaker than saturated molecules. As a result, the melting points are much lower
for unsaturated fatty acids.

14. Prostaglandin is involved in all of the following EXCEPT:

I. Relaxing and contracting smooth muscle
II. Platelet aggregation
III. hypersensitivity responses
IV. Raising body temperature
A. I only C. III only E. I & IV only
B. II only D. II & III only

Explanation: Prostaglandis likewise leukotriens are proinflammatory mediators resulting

from metabolic degradation of the arachidonic acid originating from membrane
phospholipids

15. Oxidation of ________ leads to formation of _________.

A. Saturated FAs; Ketones
B. Unsaturated FAs; Aldehydes
C. Cholesterol; Carboxylic acids
D. Triglycerides; Fatty acid soaps
E. Lipids cannot be oxidized.

Explanation: The oxidation of long-chain fatty acids to acetyl-CoA is a central energy-

yielding pathway in animals, may protists, and some bacteria. The electrons removed
during fatty acid oxidation pass through the mitochondrial respiratory chain, driving ATP
synthesis, and the acetyl-CoA produced from the fatty acids may be completely oxidized
to CO2 via the citric acid cycle.

16. The concept of "induced fit" refers to the fact that:

A. Enzyme specificity is induced by enzyme-substrate binding.
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GENERAL BIOCHEMISTRY
MTY1109
B. Enzyme-substrate binding induces an increase in the reaction entropy, thereby
catalyzing the reaction.
C. Enzyme-substrate binding induces movement along the reaction coordinate to
the transition state.
D. Substrate binding may induce a conformational change in the enzyme, which
then brings catalytic groups into proper orientation.
E. All of these

Explanation: The concept of "induced fit" refers to the fact that: A) enzyme

specificity is induced by enzyme-substrate binding. ... enzyme-substrate
binding induces an increase in the reaction entropy, thereby catalyzing the
reaction.
17. Statements:
(1) An apoenzyme, by itself, has no biochemical activity.
(2) Urease is an example of an enzyme with absolute specificity.
(3) All enzymes have names that end in -ase.
A. All three statements are true.
B. Two of three statements are true.
C. One of three statements are true.
D. None of these are true.

The ability of enzyme to bind with specific substrate or catalyze a specific set of
chemical reaction’s is called “enzyme specificity”. Some enzymes have an intrinsic
property of binding with only one substrate and catalyzing a single reaction. Enzymes
have the names that end in –ose.

18. Fischer’s ‘lock and key’ model of the enzyme action implies that:
A. The active site is complementary in shape to that of substance only after
interaction.
B. The active site is complementary in shape to that of substance
C. Substrates change conformation prior to active site interaction
D. The active site is flexible and adjusts to substrate
E. None of these

Explanation: The shape of an enzyme's active site is complementary to

the shape of its specific substrate or substrates. This means they
can fit together. Science presenter Jon Chase demonstrates the action of the
enzyme catalase, produced by the liver, in breaking down hydrogen peroxide
into water and oxygen.
19. It decreases enzyme activity by binding at a site other than the active site.
A. Reversible Competitive inhibitor
B. Reversible Noncompetitive inhibitor
C. Irreversible inhibitor
D. Positive regulator
E. Negative regulator

Explanation:In noncompetitive inhibition, an inhibitor molecule binds to

the enzyme at a location other than the active site (an allosteric site). The
substrate can still bind to the enzyme, but the inhibitor changes the shape of
the enzyme so it is no longer in optimal position to catalyze the reaction.
20. Statements:
(1) Enzymes undergo all of the reactions of proteins including denaturation.
(2) Vitamin E, a cholesterol derivative, can be synthesized in the skin by sunlight
irradiation.
 1st SUMMATIVE ASSESSMENT
GENERAL BIOCHEMISTRY
MTY1109
(3) The optimum pH for enzyme activity within the human body is always within the
physiological pH range of 7.0 to 7.5.
A. All three statements are true.
B. Two of three statements are true.
C. One of three statements are true.
D. None of these are true.

Explanation: Denaturation can be brought about in various ways. Proteins are denatured
by treatment with alkaline or acid, oxidizing or reducing agents, and certain organic
solvents Interesting among denaturing agents are those that affect the secondary and
tertiary structure without affecting the primary structure. The agents most frequently
used for this purpose are urea and guanidinium chloride.