INDUCTION COURSE PGT LDCE (PRE-WORK)

TOPIC: PROTEINS

SECTION A - MULTIPLE CHOICE QUESTIONS (1 MARK)

1. Proteins are found to have two different types of secondary structures namely α-helix and β-pleated
sheet structure, α-helix structure of protein is stabilized by
(a) peptide bonds (b) van der Waals forces (c) hydrogen bonds (d) dipole-dipole interactions

2. Each polypeptide in a protein has amino acids linked with each other in a specific sequence. This
sequence of amino acids is said to be
(a) Primary structure of proteins (b) secondary structure of proteins
(c) tertiary structure of proteins (d) quaternary structure of proteins

3. Which of the following is not a function of proteins in living organisms?

A) Storage of genetic information B) Enzymatic catalysis
C) Structural support D) Transport of molecules

4. Protein is a polymer made of

(a) carbohydrates (b) amino acids (c) nucleic acids (d) carboxylic acids

5. The specific sequence of amino acids in a polypeptide chain is known as

(a) Primary structure of proteins (b) Secondary structure of proteins
(c )Tertiary structure of proteins (d) Quaternary structure of proteins

6. Which of the following is an example of globular protein

(a) Insulin (b) Keratin (c) Myosin (d) Pectin

7. The building blocks of proteins are:

a) glucose b) glycerol c) fats d) amino acids

8. In the following questions a statement of Assertion(A) is followed by a statement of

Reason(R).Select the most appropriate answer from the options given below:
(a) Both A and R are true and R is the correct explanation ofA
(b) Both A and R are true but R is not the correct explanation of A.
(c) Ais true but R is false.
(d) A is false but R is true.
Assertion:- Insulin is a globular protein.
Reason:-Globular Proteins are water insoluble because of hydrophilic part

9. The primary structure of a protein refers to:

A) The sequence of amino acids
B) The three-dimensional arrangement of the polypeptide chain
C) The arrangement of multiple polypeptide chains
D) The formation of disulfide bonds

10. Which of the following amino acids is polar and uncharged?

A) Alanine B) Glycine C) Serine D) Valine

11. Which level of protein structure is primarily determined by hydrogen bonds between backbone
atoms?
A) Primary structure B) Secondary structure C) Tertiary structure D) Quaternary structure

12. An alpha helix and a beta sheet are examples of:

A) Primary structure B) Secondary structure C) Tertiary structure D) Quaternary structure

13. Which of the following is an example of a fibrous protein?

A) Insulin B) Myoglobin C) Collagen D) Hemoglobin

14. Which of the following is not classified as proteins:

a) Enzymes b) Antibodies c) Hormones d) Antigen

15. Which of the following is a non-polar amino acids:

a) Alanine b) Arginine c) lysine d) Serine

ANSWERS:
1. a
2. a
3. a
4. b
5. a
6. a
7. d
8. c
9. a
10. c
11. b
12. b
13. c
14. d
15. a

SECTION B- SHORT ANSWER ( 2 MARK)

1. Describe what you understand by primary structure and secondary structure of proteins?

2. Distinguish between insulin and keratin.

3. Give one example of

(a) A fibrous protein (b) A globular protein

4. Classify the following as globular or fibrous proteins.

(i) Keratin (ii) Myosin (iii) Insulin (iv) Hemoglobin

5. Name four types of intermolecular forces which stabilize structure of proteins.

6. What are essential and non-essential amino acids? Give one example of each type.

7. Mention the type of linkage responsible for the formation of the following :
(i) Primary structure of proteins (ii) Cross-linkage of polypeptide chains
(iii) a-helix formation (iv) b-sheet structure

8. Answer the following :

(i) What type of linkage is responsible for the primary structure of proteins?
(ii) Name the location where protein synthesis occurs in our body.

9. Where does the water present in the egg go after boiling the egg?

10. Explain what is meant by a peptide linkage.

ANSWERS:
1. Primary structure of proteins : Proteins may have one or more polypeptide chains. Each polypeptide
in a protein has amino acids linked with each other in a specific sequence which is known as primary
structure of protein.
Secondary structure of proteins : The conformation which the polypeptide chains assume as a result of
hydrogen bonding is called the secondary structure of the protein.

2. Insulin is a lobular protein and keratin is fibrous protein

3. Fibrous protein–Keratins and Myosin

Globular protein–Insulin and Hemoglobin.
4. Fibrous proteins are structural proteins that are made up of long and narrow strands (they are
something) example: keratin and myosin.
Globular proteins are more compact and rounded in form, and they have a functional purpose (they do
something) example: insulin and haemoglobin.

5. Hydrogen bonds, disulphide connections, van der Waals, and electrostatic forces of attraction are the
primary factors that stabilize the secondary and tertiary structures of proteins.

6. Essential amino acids : Amino acids which the body cannot synthesize are called essential amino acids.
Example : Valine, leucine etc. Therefore they must be supplied in diet.

Non-essential amino acids : Amino acids which the body can synthesize are called non-essential amino
acids. Therefore, they may or may not be present in diet.
Example : Glycine, alanine etc.

7. Peptide linkage, hydrogen bonding

8. peptide linkage & proteins are formed in ribosomes of cell.

9. In an egg, denaturation of protein is the coagulation of albumin present in the white of an egg. When
an egg is boiled in water, the globular proteins present in it change to a rubber like insoluble mass which
absorbs all the water present in the egg by making hydrogen bond with it.

10. Peptide linkage: A peptide linkage is an amide linkage formed between – COOH group of one α-
amino acid and NH2 group of the other a-amino acid by loss of a molecule of water.

SECTION C- SHORT ANSWER ( 3 MARK)

1. Define the following terms as related to proteins : (i) Peptide linkage (ii) Primary structure (iii)
Denaturation

2. Write difference between tertiary and quartenary structure with diagram.

3. Coagulation of egg white on boiling is an example of the denaturation of protein. Explain it in terms
of structural changes.

4. Amino acids may be acidic, alkaline or neutral, How does this happen?
5. Describe zwitter ion in detail.

6. Compare and contrast denaturation and coagulation of proteins.

7. State difference between globular and fibrous proteins.

8. Amino acids behave like salts rather than simple amines or carboxylic acids. Explain.

9. Protein found in a biological system with a unique three-dimensional structure and biological activity
is called a native protein. Protein denaturation occurs when a protein in its native form is subjected to a
physical change like a change in temperature or a chemical change like a change in pH. Explain the
cause.

10. Amino acid show amphoteric behavior. Give reason.

ANSWERS:

1. Peptide linkage: A peptide linkage is an amide linkage formed between – COOH group of one α-amino
acid and NH2 group of the other a-amino acid by loss of a molecule of water.

Primary Structure: The primary structure of a protein refers to the linear sequence of amino acids linked
by peptide bonds.

Denaturation: Denaturation is the disruption of a protein's secondary, tertiary, or quaternary structure,

resulting in the loss of its biological activity. It can be caused by heat, pH extremes, organic solvents, or
mechanical agitation. Example: Cooking of egg whites causes denaturation of the albumin protein.

2. Tertiary Structure: Tertiary structure refers to the overall three-dimensional shape of a protein. It is
stabilized by interactions between amino acid side chains (hydrophobic interactions, hydrogen bonds,
disulfide bonds, etc.).

Quaternary Structure:- Quaternary structure refers to the arrangement of multiple protein subunits
(polypeptide chains) in a multi-subunit complex. It involves interactions between different polypeptide
chains (subunits).

3. When the egg white is boiled, the soluble globular protein albumin is converted into insoluble fibrous
protein. During this denaturation, (i) biological activity is lost and (ii) secondary and tertiary structures of
albumin protein are destroyed while the primary structure (representing the sequence of amino acids)
remains intact.

4. Amino acids can be broadly classified into three classes i.e. acidic, alkaline and neutral amino acids
depending on the number of —NH2 group and — COOH group.
Acidic amino acids : Those a-amino acids such as aspartic acid, asparagine and glutamic acid which
contain two -COOH groups and one -NH2 group are called acidic amino acids.

Alkaline or Basic amino acids : Those a-amino acids such as lysine, arginine and histidine which contain
two -NH2 groups and one -COOH group, are called basic amino acids.

Neutral amino acids : Those a-amino acids such as glycine, alanine, valine etc. which contain one -
NH2 and one – COOH group, are called neutral amino acids.

5. Amino acids contain amino and carboxylic acid group, In aqueous solution, the carboxyl group can
lose a proton and amino group can accept a proton, giving rise to a dipolar ion known as zwitter ion.This
is neutral but contains both positive and negative charges

6. Denaturation: Denaturation is the disruption of a protein's secondary, tertiary, or quaternary

structure, resulting in the loss of its biological activity. It can be caused by heat, pH extremes, organic
solvents, or mechanical agitation. Example: Cooking of egg whites causes denaturation of the albumin
protein.

Coagulation: Coagulation refers specifically to the irreversible aggregation of denatured protein

molecules, leading to the formation of a solid or gel-like mass. Example: Formation of curd from milk
involves coagulation of casein proteins under acidic conditions.

7.
S.NO. Globular Protein Fibrous Protein

1 they form α‐helix structure they have β‐pleated structure

2 They are water soluble. they are water insoluble

3 They involve H bonding. they have strong intermolecular forces of

attraction

8. Amino acids behave like salts rather than simple amines or carboxylic acids due to the presence of
both acidic (-COOH) and basic (-NH2) groups. In solution, the -COOH group can lose a proton, and an
amine group can accept a proton, giving rise to a dipolar ion called the Zwitter ion.

9. Due to physical and chemical changes, hydrogen bonds in proteins are disturbed. Due to this, globules
unfold, and, the helix gets uncoiled, the protein loses its biological activity. This is known as the
denaturation of proteins.
 10. Due to presence of carboxylic acid and amino group in the same molecule or due to formation of
zwitter ion or dipolar ion, amino acid show amphoteric behavior.

SECTION D- CASE BASED QUESTIONS (4 MARK)

1. Protein found in a biological system with a unique three-dimensional structure and biological activity
is called a native protein. Protein denaturation occurs when a protein in its native form is subjected to a
physical change like a change in temperature or a chemical change like a change in pH..α Helix is a
secondary structure of proteins formed by twisting the polypeptide chain into right-handed screw-like
structures.
i) Explain the cause of denaturation.
ii) Which type of interactions is responsible for making the α -helix structure stable?
iii) Which structure of proteins remains intact during the denaturation process?
iv) What type of structure is α -helix and β-pleated structures of proteins?

2. The Amino acids, which are required in our body but can’t be synthesized by our body are called
essential amino acids. Amino acids can be classified as alpha, beta, gamma, delta, and so on, depending
upon the relative position of the amino group concerning the carboxyl group.

i) What are alpha amino acids?

ii) Which type of amino acids forms the polypeptide chain in proteins?
iii) Give any two examples of alpha amino acids.
iv) What are non-essential amino acids?

ANSWERS:
1. i) Due to physical and chemical changes, hydrogen bonds in proteins are disturbed. Due to this,
globules unfold, and, the helix gets uncoiled, the protein loses its biological activity. This is known as the
denaturation of proteins.
ii) In α helix, a polypeptide chain is stabilised by forming hydrogen bonds between the −NH− group of
amino acids in one turn with the >C−O groups of amino acids belonging to adjacent turn.
iii) Primary structure remains intact during the denaturation process.
iv) Secondary structures
2. i) The α-amino acids are the amino acids whose one carbon contains both the amino group (NH2)
and carboxyl group (COOH). Such type of carbon is called α-carbon. Thus, the amino acid that contains
an α-carbon is called an α-amino acid.
ii) α amino acid forms a polypeptide chain by eliminating water molecules.

SECTION E- LONG ANSWER ( 5 MARK)

1. Explain the terms primary and secondary structure of proteins. What is the difference between the
alpha-helix and beta-pleated sheet structure of proteins?
2. Differentiate between fibrous proteins and globular proteins. What is meant by the denaturation of a
protein?
3. Explain tertiary structure of Protein.
4. Explain the primary, secondary, tertiary, and quaternary structures of proteins.

ANSWERS:
1. Protein primary structure is the linear sequence of amino acids in a peptide or protein. In contrast,
Secondary structure refers to regular, recurring arrangements in the space of adjacent amino acid
residues in a polypeptide chain. It is maintained by hydrogen bonds between amide hydrogens and
carbonyl oxygens of the peptide backbone. The major secondary structures are α-helices and β-
structures.

2.
Globular Proteins Fibrous Proteins

1. Polypeptide chains of fibrous proteins consist of

1. Globular proteins have almost spheroidal
thread like molecules which tend to lie side by side
shape due to folding of the polypeptide chain.
to form fibres.

2. Globular proteins are soluble in water. 2. Fibrous proteins are insoluble in water.
3. Globular proteins are sensitive to small
changes of temperature and pH. Therefore 3. Fibrous proteins are stable to moderate changes
they undergo denaturation on heating or on of temperature and pH.
treatment with acids/bases

4. They possess biological activity that’s why 4. They do not have any biological activity but serve
they act as enzymes. as chief structural material of animal tissues.

Example: Maltase, invertase etc., hormones

Example: Keratin in skin, hair, nails and wool,
(insulin) antibodies, transport agents
collagen in tendons, fibroin in silk etc.
(haemoglobin), etc.

Denaturation of protein : Due to coagulation of globular protein under the influence of change in
temperature, change in pH etc., the native shape of the protein is destroyed and biological activity is lost
and the formed protein is called denaturated proteins and the phenomenon is denaturation.

3. Tertiary structure of proteins: The tertiary structure of proteins represents overall folding of the
polypeptide chains i.e., further folding of the secondary structure. It gives rise to two major molecular
shapes viz. fibrous and globular. The main forces which stabilize the 2° and 3° structures of proteins are
hydrogen bonds, disulphide linkages, van der Waals and electrostatic force of attraction. Explanation
with diagram.

4. Primary Structure: The primary structure of a protein refers to the linear sequence of amino acids
linked by peptide bonds.

Secondary Structure: Secondary structure refers to the local folded structures that form within a
polypeptide chain. The two main types are alpha helices and beta sheets, stabilized by hydrogen bonds
between backbone atoms.

Tertiary Structure: Tertiary structure refers to the overall three-dimensional shape of a protein. It is
stabilized by interactions between amino acid side chains (hydrophobic interactions, hydrogen bonds,
disulfide bonds, etc.).

Quaternary Structure:- Quaternary structure refers to the arrangement of multiple protein subunits
(polypeptide chains) in a multi-subunit complex. It involves interactions between different polypeptide
chains (subunits).
SUBMITTED BY:
Monika Vaishnav
PGT Chemistry
KV NO. 1 Vasco da Gama
Goa