LECT – 11- 15 AMINO ACIDS – PROTEINS

OBJECTIVE QUESTIONS AND ANSWERS

1. The bond formed between two amino acid molecules is

a. peptide bond
b. sulfur linkage
c. ionic bond
d. coordinate covalent bond

2. The number of amino acids that have hydrophobic side chains are

a. 7
b. 8
c. 9
d. 10

3. The sulfur atom of cysteine is involved in formation of

a. sulfide group
b. sulfhydryl group
c. sulfite group
d. Sulphates

4. Polar amino acids are usually found

a. on the surface of proteins

b. inside the core of proteins

c. at the sides of proteins

d. can be present anywhere in proteins

5. The amount of amino acid residues in proteins ranges from

a. 50-2000

b. 2000-4000

c. 4000-6000

d. 7000-10,000
6. The interactions which holds and stabilizes the sub units in 4° structure of proteins
are
a. hydrophilic interactions

b. hydrogen bonding

c. hydrophobic interactions

d. Ionic bonding

7. The process of folding depends upon the

a. solvent

b. the concentration of salts

c. pH

d. all of above

8. Which among the following is a non-essential amino acid?

a. Serine

b. Threonine

c. Lysine

d. Histidine

9. Which of the following is an imino acid?

a. Alanine

b. Glycine

c. Proline

d. Serine

10. Which among the following is both glucogenic and ketogenic?

a. Isoleucine

b. Leucine

c. Lysine

d. Histidine
11. Number of chiral centers in isoleucine is

a. 1

b. 2

c. 3

d. 4

12. Unfolding of a protein can be termed as

a. Renaturation

b. Denaturation

c. Oxidation

d. Reduction

13. β-pleated sheets are the examples of

a. Primary structure

b. Secondary structure

c. Tertiary structure

d. Quaternary structure

14. A coiled peptide chain held in place by hydrogen bonding between peptide bonds in
the same chain is

a. Primary structure

b. α-helix

c. β-pleated sheets

d. Tertiary structure

15. A structure that has hydrogen bonds between polypeptide chains arranged side by
side is

a. Primary structure

b. α-helix

c. β-pleated sheets

d. Tertiary structure
16. Fibroin is rich in

a. Alanine and Glycine

b. Alanine

c. Glycine

d. Pro

17. Which of the following is abundantly found in collagen?

a. Glycine

b. Serine

c. Alanine

d. Tryptophan

18. _________ is a heme protein is a component of the respiratory chain of

mitochondria.

a. Ribonuclease

b. Lysozyme

c. Cytochrome c

d. Myoglobin

19. The enzyme which can lyse, or degrade, bacterial cell walls, so it serves as
bactericidal agent.

a. Ribonuclease

b. Lysozyme

c. Cytochrome c

d. Myoglobin

20. ___________ an alkylating agent cannot denature protein

a. Iodoacetic acid

b. SDS detergent

c. Urea

d. Heating to 90°C
21. Which amino acid has imidazole imidazole ring?

a. Alanine

b. Leucine

c. Trysoine

d. Histidine

22. The nonprotein component is called a

a. Cofactor

b. Coenzyme

c. Prosthetic group

d. Nonprosthetic group

23. A protein molecule combined with its prosthetic group is referred to as a

a. Holoprotein

b. Hemoprotein

c. Apoprotein

d. Phosphoprotein

24. Aromatic amino acids have an absorption maxima at

a. 260 nm

b. 250 nm

c. 280 nm

d. 270 nm

25. These amino acids can be synthesized in the body but the rate of synthesis is lesser than
the requirement

a. Essential amino acids

b. Aromatic Amino acids

c. Nonessential Amino acids

d. Semi essential Amino acids

26. _________ are basic units of protein.

a. Amino acids

b. Polypeptides

c. Ampolytes

d. Zwitter ions

27. The amino acids which is synthesized from glutamic acid

a. Amino butyrate

b. Gamma amino butyric acid (GABA)

c. Amino purinate

d. Gamma carboxylglutamate

28. These amino acids serves as precursors gluconeogenesis for glucose formation

a. Ketogenic

b. galactogenic

c. glucogenic

d. lactogenic

29. _____________are also the constituents of alkaloids

a. Peptides

b. Dipeptide

c. Oligopeptide

d. Tripeptide

30. Peptides also acts as growth factors in

a. Vit K

b. Vit B

c. Vit A

d. Vit C
31. Side chains which have pure hydrocarbon alkyl groups (alkane branches) or aromatic
(benzene rings) are

a. Non polar

b. basic

c. polar

d. acidic

32. An intramolecular neutralization reaction leads to a salt-like ion called

a. Ampolytes

b. Amphipathic

c. Zwitter ions

d. Isoelectric point

34. ______________ forms the major nitrogenous constituent of plants

a. Zwitter ions

b. Protein

c. Peptide

d. Amino acids

35. ____________ assimilated by Plants

a. D -Amino acids

b. Hydroxyl Amino acids

c. Sulphur Amino acids

d. L - Amino acids

36. _________is precursor for Auxin synthesis.

a. L-Phenylalanine

b. L – Tyrosine

c. L – Tryptophan
 d. L – Histidine

37. The amino acids which induces synthesis of flower and fruit related hormones.

a. L-Serine

b. L – Arginine

c. L – Valine

d. L – Threonine

38. Which amino acids are fundamental metabolites in the process of formation of vegetable
tissue and chlorophyll synthesis

a. Alanine and Aspartic acid

b. Leucine and Ascorbic acid

c. Glycine and Glutamic acid

d. Cysteine and Aspargine

39. ___________ acts as a cytoplasm osmotic agent of the “Guard Cell”.

a. L-Glutamic acid

b. L – Aspargine

c. L – Glutamine

d. L – Aspartic acid

40. Which amino acids improve the quality of frutis

a. L-Glutamic acid, L-Valine, L- serine

b. L – Arginine, L-Alanine, L- Lysine

c. L-Alanine, L-Valine, L-Leucine

d. L – Aspartic acid, L-Alanine, L- Leucine

41. A molecule or ion that can react both as an acid as well as a base.

a. Amphoteric nature

b. Zwitter ions

c. Isoelectric pH
 d. Schiff’s rule

42. A particular molecule carries no net electrical charge or is electrically neutral

a. Amphoteric nature

b. Zwitter ions

c. Isoelectric pH

d. dissociation constant

43. The process by which a protein structure assumes its functional shape or conformation.

a. misfolding

b. Acid folding

c. Base folding

d. Protein folding

44. Spherical in shape and occur mainly in plants, esp., in seeds and in leaf cells

a. Fibrous protein

b. Globular protein

c. chromoprotein

d. Amyloprotein

45. All protein solutions rotate the plane of polarized light to the left

a. Levororotatory

b. Dextrorotatory

c. D & L form

d. All of the above

46. Thread-like or ellipsoidal in shape and occur generally in animal muscles

a. chromoprotein

b. Globular protein

c. Fibrous protein

d. Amyloprotein
 47. The final shape of the protein complex is once again stabilized by various interactions,
including

a. Hydrogen bonding

b. Disulfide bridges

c. Salt bridges

d. All of the above

48. A chain-like biological molecule, such as a protein or nucleic acid

a. Motifs

b. Structural Motif

c. Zinc-finger motifs

d. None of the above

49. Proteins that assist the covalent folding or unfolding and the assembly or disassembly of
other macromolecular structures.

a. molecular chaperones

b. Protein domain

c. Heat shock proteins

d. All of the above

50. A single polypeptide chain "backbone" with one or more protein secondary structures is

a. Chaperones

b. Protein domain

c. Nucleoproteins

d. misfolded protein

Match the following

Aliphatic Amino acids a. Arginine - 2

Basic Amino acids b. Glutamic acid - 4
Imino acids c. Glycine - 1
Acidic Amino acids d. Proline - 3
 a. Tryptophan -2

b. Chorismate - 4

c. Phenylalanine - 1

d. Tyrosine -3

Glutelins a. Thymus - 4
Oryzenin b. Maize - 3
Zein c. Wheat - 1
Histone d. Rice - 2

Histidine a. Cucumber -3
Isoleucine b. Beets - 1
Lysine c. Soy protein -4
Methionine (+ Cysteine) d. kidney beans -2

Phenylalanine (+ Tyrosine) a. Plant hormone precursor -2

Tryptophan b. Nonprotein Amino acids -4
Tyrosine c. Neurotransmitters - 1
GABA d. Plant cell Signaling - 3
Primary (1ᵒ) a. Ligand binding -3
Secondary (2ᵒ) b. Covalent bonding - 4
Tertiary (3ᵒ) c. hydrogen bonding -2
Quaternary (4ᵒ) d. Peptide bond formation - 1

Xanthoproteic Test a. Proteins -2

Biuret Test b. Phenylalanine -1
Hopkins cole Test c. Arginine - 4
Sakaguchi Test d. Tryptophan - 3

Descriptive Questions

1. What are proteins?

Proteins are molecules made up of sequences of amino acids bound by a peptide bond

2. What is the importance of proteins for living organisms?

Proteins play a fundamental role in nearly all biological processes. Due to their
diversity, they can take on many different configurations and can play varied roles in
cells and tissues.

3. What units are proteins composed of?

The units that make up proteins are amino acids.

4. What is an oligopeptide? How is it different from a polypeptide?

The peptide molecule is the molecule formed by the bonding of amino acids
through the peptide bond. An oligopeptide is a peptide composed of few amino acids
(oligo = few). Polypeptides are peptides that contain many amino acids (poly =
many), in general more than 50.

5. Does every amino acid have a central carbon atom? To which organic group is
that central carbon atom bound?
 A carboxyl group –COOH, an amine group – NH₂, an hydrogen atom –H and a
variable radical -R are necessarily bound to the central carbon atom of an amino acid.

6. How can amine groups be classified?

Amines can be classified into primary amines, in which one –R (variable radical) is
attached to a –NH₂; secondary amines, in which one hydrogen atom of the NH₂ is
substituted by another –R, thus leaving two –R; and tertiary amines, in which there
are no hydrogen atoms bound to the nitrogen and with three –R instead.

7. What is the molecular structure of a carboxyl group?

Carboxyl groups (–COOH) have one carbon atom attached to one hydroxyl group
through a simple bond and to one oxygen atom via a double bond. The carbon atom’s
other bond site is available to other substances.

8. What is the flat structural representation of an amino acid molecule?

An amino acid molecule has a central carbon atom to which a carboxyl group is
bound on one side and to which a –R (variable radical) is bound on the opposite side.
Perpendicular to those ligands, an amine group is bound to the central carbon atom on
one side, and a hydrogen atom is bound on its opposite side.

The bond between the carboxyl group and a carbon atom in which a hydrogen atom is
laterally attached is the reason for the name “acid” in amino acids. The bond between
an amine group and the central carbon gives the name “amino.”

9. What is the importance of the –R group (variable radical) in an amino acid

molecule?

The –R group, also called a side-chain, is the variable part of the amino acid
molecule. The –R g2roup can be a complex chain of carbon atoms, a substitute
methyl group (in this case forming the amino acid alanine) or even a sole hydrogen
atom (forming glycine, the simplest amino acid). Therefore the –R group is important
because it is what distinguishes the different amino acids.
10. How can the binding of two amino acids into a peptide formation be described?

A peptide is formed when a carbon atom from the carboxyl group of one amino acid is
connected to the nitrogen atom of the amine group of another amino acid. Through that
bond, the hydroxyl group of the carboxyl group and one hydrogen atom of the amine are
lost resulting in the release of one water molecule.

11. What is the bond between two amino acids called?

The chemical bond between two amino acids is called a peptide bond.

12. How the –R groups bound to the central carbon atoms involved in the bond
between amino acids?

The peptide bond connects the nitrogen atom of the amine group of one amino acid to the
carbon atom of the carboxyl group of another amino acid, releasing one molecule of
water. Therefore, the –R groups do not participate in that bond.

13. How the –H groups bound to the central carbon atoms involved in the peptide
bond?

The central carbon atoms, the –R groups and the hydrogen atoms attached to the central
carbon atoms do not participate in the peptide bond.

14. When the amine and the carboxyl groups attached to central carbon atoms
involved in the bond between amino acids?

Yes. The nitrogen of the amine group of one amino acid binds to the carbon atom of the
carboxyl group of the other amino acid. The water molecule released from the formation
of the peptide bond thus contains one hydrogen atom from the amine and an oxygen atom
and the other hydrogen atom from the carboxyl group.

15. Do the chemical reactions to bind amino acids incorporate or release atoms?
What are the chemical entities incorporated or released during this reaction?

The binding of amino acids via the peptide bond releases atoms. They are released in the
form of one molecule of water.
16. If the same amount of amino acids create different proteins?

Different proteins with the same total number of amino acids may exist. In such cases,
the difference depends on the types of amino acids or on the sequence in which they form
the protein.

17. Is the protein with the same number of their respective amino acid components
necessarily identical?

While many proteins share the same number of each of their different amino acid
components, for example, 50 alanine, 70 glycine and 20 histidine, the sequences in which
these amino acids are connected may be very different. Therefore, if two or more proteins
have the same number of each of their amino acid components, they are not necessarily
identical.

18. What is the essential condition for one protein molecule to be identical to
another protein molecule?

For a protein molecule to be identical (exactly) to another protein molecule, it is

necessary for the sequences of amino acids that form them to be identical.

19. What is the primary structure of a protein? What is the importance of the primary
structure?

The primary structure of a protein is the linear sequence of amino acids that form the
molecule.

The primary structure is the basis of identity of the protein. Modification of only one
amino acid in the primary structure creates a different protein. This different protein can
be inactive or can even have other biological functions.

20. What is the secondary structure of a protein?

The secondary structure of a protein is generated by the way in which its amino acids
interact through the intermolecular bond. These interactions create a spatial conformation
of the polypeptide chain. The two most studied secondary conformations of proteins are
the alpha-helix and the beta-sheet.

21. What is the difference between alpha-helix and beta-sheet protein

conformations?

Alpha-helix and beta-sheet conformations are the two main types of secondary structures
of a protein molecule. Depending on the primary protein structure, its secondary structure
can be of one type or the other.

In the alpha-helix structure, the polypeptide curls longitudinally through the action of
hydrogen bonds, forming a spiral or helix. In the beta-sheet conformation, the protein is
more extended and the hydrogen bonds form a zig-zag-shaped protein structure called a
beta-strand. Many beta-strands put together make a beta-sheet.

22. What is the tertiary structure of a protein? What are the main types of tertiary
structures?

The tertiary structure of a protein is a spatial conformation in addition to the secondary

structure, in which the alpha-helix or the beta-sheet folds itself up. The forces that
maintain the tertiary structure are generally interactions between the –R groups of the
amino acids, other parts of the protein and the water molecules of the solution.

The main types of tertiary structure of proteins are globular proteins and fibrous proteins.

23. What is the quaternary structure of a protein? Do all proteins have a

quaternary structure?

The quaternary structure of a protein is the spatial conformation caused by interactions

between the polypeptide chains that form the protein.

Only proteins made up of two or more polypeptide chains have a quaternary structure.
Insulin (two chains), hemoglobin (four chains) and immunoglobulins (antibodies, four
chains) are some examples of protein with a quaternary structure.
24. What is protein denaturation? Are there any changes in the primary structure
when a protein is denatured?

The secondary, tertiary and quaternary structures of a protein are spatial structures.
Denaturation is a modification in any of these spatial structures that makes the protein
deficient or biologically inactive.

After denaturation the primary protein structure is not affected.

25. How can denaturation be classified according to its reversibility?

Protein denaturation can be reversible or irreversible. That means that it may be possible
or impossible for the protein to regain its original spatial conformation.

26. What are the factors influences that can lead to protein denaturation?

Protein denaturation can be caused by temperature variation, pH change, changes in the

concentration of surrounding solutes and by other processes. Most proteins denature after
certain elevations in temperature or when in very acidic or very alkaline solutions. This is
one of the main reasons that it is necessary for organisms to mantain a stable temperature
and pH.

27. Does a change in the primary, secondary or tertiary structure of a protein

normally have consequences for their function?

Any changes in the structure of a protein are relevant if they alter its biological activity.
Changes in the primary structure of a protein are the most important because they are
modifications in the composition of the molecule, and that composition determines all the
other structures of the protein.

28. What is the difference between essential and nonessential amino acids?

Essential amino acids are those that the body is not able to synthesize and which need to
be ingested by the individual. Nonessential amino acids are those that are produced by
the body.
There are living species that produce every amino acid they need. For example, the
bacteria Escherichia coli does not have essential amino acids. Other species, like
humans, need to obtain essential amino acids from their diet. Among the twenty different
known amino acids that form proteins humans can produce twelve of them and the
remaining eight needs to be taken from proteins ingested through food.

The essential amino acids for humans are phenylalanine, histidine, isoleucine, lysine,
methionine, threonine, tryptophan and valine

29. Define Isoelectric point (pI) of amino acids

Isoelectric point is the point along the pH scale where the amino acid has a net zero
charge. Consider glycine. Look at the equilibrium below; as we add hydroxide ions—in
other words, raise the pH—different charged forms of glycine exist. Form B has a net
zero charge and is called a zwitterion. Form A has a net charge of +1, and form C has a
net charge of -1.

30. Define Chaperone

Proteins that assist the covalent folding or unfolding and the assembly or disassembly
of other macromolecular structures.
Define the following terms:

a. Protein, Amino acids, Polypeptide chain

b. fibrous protein
c. globular protein
d. prosthetic group
e. apoprotein
f. aliphatic hydrocarbon
g. Neurotransmitter
h. asymmetric carbon
i. chiral carbon
j. stereoisomer
k. protein motif
l. conjugated protein
m. Dynein
n. Zwitterions
o. Electrophoresis
p. optical isomer
q. isoelectric point
r. peptide bond
s. disulfide bridge
t. denaturation
u. holoprotein
v. Amphoteric nature
w. SDS
x. Renaturation
y. Glutelin
z. Zein

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1. Charges on amino acids
2. Explain the structure of amino acids
3. Classify amino acids. Give examples for each group
4. Describe proteins
5. Describe the structure of protein
6. Explain the function of proteins
7. Explain the Classification of proteins based on Solubility, shape, biological
importance
8. Describe products of amino acids
9. Classification of Amino acids based on polarity
10. Difference between essential and non essential amino acids
11. Depict the properties of Amino acids and proteins
12. Write a short note on the isoelectric pH of protein and its importance
 13. Ninhydrin Test
14. Define Glutathione
15. Define α- helix. What are the features of α- helix
16. Explain in details about the force of attraction involved in tertiary structure of
proteins
17. Discuss about Seed Storage protein
18. Write a short note on Artificial peptide and protein sweeteners
19. Amphoteric nature of amino acids
20. Difference between fibrillar and globular proteins

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 Hydrophobic amino acids have nonpolar side chains, such as alkyl groups
or aromatic groups.
 Hydrophilic—neutral—amino acids contain polar side chains, such as
hydroxyl-OH-OH negative, O, H, and sulfhydryl,-SH –SH negative, S, H,
groups.
 Hydrophilic—acidic—amino acids have side chains that contain
carboxylic acid,-COOH-COOH negative, C, O, O, H, groups.
 Hydrophilic—basic—amino acids have side chains that contain amine-
NH2 negative, N, H, start subscript, 2, end subscript, groups.
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Forces that keep the different protein structures together

Level of protein
structure Interactions that stabilize the structure

Primary Covalent bond (amide/peptide bond)

Secondary Hydrogen bonds

Ionic bonds, disulfide bonds, hydrophobic interactions, hydrogen

Tertiary bonding

Ionic bonds, disulfide bonds, hydrophobic interactions, hydrogen

Quaternary bonding
Amino Acids are precursors or activators of phytohormones and growth substances. L -
Methionine is precursor of ethylene and of growth factors such as Espermine and
Espermidine, which are synsthesized from 5 - Adenosyl Methionine.

L - Tryptophan is precursor for Auxin synthesis. L - Tryptophan is used in plants in L -

Form only. L - Tryptophan is available only if hydrolysis of Protein is carried out by enzyme.

L - Arginine induces synthesis of flower and fruit related hormones.