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Cell Biology: Digestion & Lipid Structures

The document contains sample exam questions about biological molecules including proteins, lipids, and amino acids. It asks students to describe how chicken protein is digested, identify the type of fat likely found in chicken soup, explain the physical differences between butter and olive oil, describe the structures of phospholipids and cholesterol, identify functional groups in the amino acid threonine, explain why partially hydrogenated oil is unhealthy, give an example of a biological macromolecule found in mussels and its medical application, and explain how protein structures can differ. The document provides figures and tables to support the questions, and tests students' understanding of protein structure levels and the features that define each level.

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7 views4 pages

Cell Biology: Digestion & Lipid Structures

The document contains sample exam questions about biological molecules including proteins, lipids, and amino acids. It asks students to describe how chicken protein is digested, identify the type of fat likely found in chicken soup, explain the physical differences between butter and olive oil, describe the structures of phospholipids and cholesterol, identify functional groups in the amino acid threonine, explain why partially hydrogenated oil is unhealthy, give an example of a biological macromolecule found in mussels and its medical application, and explain how protein structures can differ. The document provides figures and tables to support the questions, and tests students' understanding of protein structure levels and the features that define each level.

Uploaded by

Eng
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd

202105

UNIVERSITI TUNKU ABDUL RAHMAN


CENTRE FOR FOUNDATION STUDIES

FHSC1214 FUNDAMENTALS OF CELL BIOLOGY

TUTORIAL 2
BIOLOGICAL MOLECULES II

[Source: Final Assessment for Apr 2021]


Q1. (a) Campbell Soup Company, founded in 1869, makes a range of soups and
simple meals. Figure 1.1 shows a printed food label of its ‘Chicken with Rice
Soup’ in the 1960s.

Figure 1.1

(iii) With reference to protein structure, explain how chicken in the above
soup is digested in the human digestive system for its nutrient to be
absorbed by the human body. Answer in not more than 140 words.
(6
marks)
In the stomach, HCl and pepsin hydrolyses protein (quaternary
structure) into polypeptide (tertiary structure). When it reaches
duodenum, trypsin breaks down the polypeptide into dipeptide
(secondary structure). In the ileum, erepsin hydrolyses dipeptide into
amino acid (primary structure) by breaking down the peptide bond. The
amino acid will be adsorbed directly into the bloodstream.

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202105

(iv) State the type of fat (saturated/ unsaturated) that is most likely to be
found in the above soup. Describe the structure of this fat. Answer in
not more than 80 words. (5 marks)
Saturated fat. It composed of glycerol and 3 fatty acids. The 3 fatty
acids are joined to glycerol by an ester linkage. It has the maximum
number of hydrogen atoms bind to the carbon skeleton and is said to be
fully hydrogenated. Hence, it contains only single bonds in the carbon
chain. The space model of saturated fat does not kink and bend. Thus, it
is solid at room temperature.

[Source: Final Assessment for Jan 2020 (truncated)]


Q2. Butter and olive oil are both used in western cooking. Account for the physical
differences of these fats. Answer in not more than 100 words. (8 marks)

Butter is saturated fat. It has a solid consistency at room temperature. It has a high
melting point. It has only single bonds between carbon atoms.
Olive oil is unsaturated fat. It has a liquid consistency at room temperature. It has a
low melting point. It has double bonds between carbon atoms.

[Source: Final Assessment for May 2020]


Q3. (a) A cell is the smallest structural and functional unit of life. Describe the
structure of TWO (2) important lipids found in a cell. Answer in not more than
80 words.
(6 marks)
Phospholipid and cholesterol/steroid. Phospholipid has double layer and is
made up of 2 fatty acids and a phosphate group which is attached to the
glycerol. Steroid contains 4 fused rings (C-ring) and contains hydrophobic part.

(b) Figure 1 shows the molecular structure of threonine, one of the amino acids.
Identify THREE (3) chemical groups present in threonine and discuss their
importance in the formation of protein structures. Answer in not more than 80
words. (6 marks)

Figure 1

Carboxyl group, amino group and methyl group. Amino group releases OH-
group during dehydration synthesis to form water. These groups involved in
the peptide bond formation to bind amino acid. They form hydrogen bond,
ionic bond, Van der waals force, hydrophobic interaction and disulphide
bridges.

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202105

[Source: Final Assessment for Dec 2020]


Q4. (a) Based on your understanding on lipid, briefly explain why the product shown
in Figure 2 is bad for your heart. Answer in not more than 50 words. (3 marks)

Figure 2

Contain hydrogenated oil. This oil contains trans C=C conformation. It


will lead to the build up of fatty deposits in arteries. It leads to
cardiovascular disease.

(b) State ONE (1) biological macromolecule that is present in mussels and
describe its properties. Give ONE (1) application in the medical field. Answer
in not more than 60 words.
(3 marks)
Protein. The protein is found in its muscles and byssal thread. It is used to
make surgical glue to replace surgical thread.

(c) Proteins are made from 20 amino acids in random combination as determined
by the gene. Briefly explain how proteins can differ from one to another.
Answer in not more than 80 words.
(4 marks)
Sequence of amino acids. Length of the polypeptide/no. of amino acid.
Different types of amino acid. Different interaction between R groups.
Different 3D shape of protein.

[Source: Final Examination for May 2018]

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202105

Q5. There are four levels of protein structure, which are primary, secondary. Tertiary and
quaternary. Table 1 shows a set of features used when describing the structure of
protein such as hemoglobin.
Table 1
Features Letter
Hydrogen bonds A
Peptide bonds B
α and ß subunits C
The sequences of amino acids D
The initial folding of the polypeptide chain E
The overall 3D shape F
Ionic bonds G

Based on the table, select the letters that match each of the following descriptions.
There may be more than one feature.

(a) Feature found in the primary structure of protein. (2 marks)


B and D

(b) Feature found in the secondary structure of protein that are not present in the
primary structure. (2 marks)
A and E

(c) Feature found in tertiary structure of protein that are not present in the primary
and secondary structures. (2 marks)
G and F

(d) Feature found only in the quaternary structure of protein. (1 mark)


C

Common questions

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The interactions between the carboxyl group, amino group, and methyl group in threonine contribute to protein structure formation by facilitating peptide bond formation and stabilizing the protein's structure. The amino group participates in dehydration synthesis, releasing an OH- group to form water, which is critical in binding amino acids through peptide bonds. These groups also form hydrogen bonds, ionic bonds, Van der Waals forces, hydrophobic interactions, and disulfide bridges, contributing to the protein's overall stability and structure .

The quaternary structure of proteins differs from other structural levels by involving multiple polypeptide chains, or subunits, that assemble into a functional complex. In hemoglobin, this includes α and β subunits that work together to enable efficient oxygen transport, unlike primary, secondary, or tertiary structures which involve individual chains and their respective formations .

Amino acid sequences directly influence a protein's three-dimensional shape as they determine the folding pattern via interactions such as hydrogen bonds, ionic bonds, and hydrophobic effects. These interactions guide the polypeptide chain in adopting specific conformations, thereby affecting the protein's overall geometry and functional properties .

Peptide bonds, formed between amino acids during protein synthesis, establish the primary structure, while interactions between R groups influence a protein's final shape and function. The sequence and variety of these amino acids, combined with interactions like hydrogen bonding, ionic bonding, and Van der Waals forces among R groups, result in diverse protein structures and functions, reflecting differences in protein complexity and activity .

Phospholipids and cholesterol are crucial for cell membranes as they maintain structural integrity and fluidity. Phospholipids form a bilayer with hydrophilic heads and hydrophobic tails, creating a semi-permeable membrane, while cholesterol modulates membrane fluidity and stability by fitting between phospholipids, preventing them from packing too tightly and maintaining membrane flexibility .

Hydrogenated oils contain trans C=C bonds, which can lead to the buildup of fatty deposits in arteries. This accumulation can restrict blood flow and contribute to cardiovascular disease, posing significant health risks to heart health .

Saturated fats, such as those in butter, have only single bonds between carbon atoms, allowing for a linear, tightly packed structure, which makes them solid at room temperature. In contrast, unsaturated fats like olive oil contain double bonds, creating kinks that prevent tight packing, rendering them liquid at room temperature .

Trypsin plays a crucial role in digesting proteins by breaking down polypeptides in the duodenum into smaller dipeptides. This enzymatic activity decreases the complexity of proteins, enabling further breakdown into amino acids by erepsin in the ileum, which can then be absorbed directly into the bloodstream for use by the body .

The protein in mussels, particularly in the muscles and byssal threads, is utilized in making surgical glue, which is an alternative to traditional surgical thread. This application takes advantage of the protein's adhesive properties, providing benefits in surgeries by minimizing tissue damage and enabling quicker healing .

Phospholipids consist of two fatty acids, a phosphate group, and glycerol, forming a bilayer crucial to membrane structure. In contrast, steroids like cholesterol have four fused hydrocarbon rings, providing rigidity and influencing membrane fluidity. These structural differences enable phospholipids to form barriers and steroids to modulate membrane properties and signaling activities .

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