BIOLOGY STPM SEMESTER 1

CHAPTER 1: BASIC CHEMISTRY OF CELL

1. Describe four properties which render water to be an important medium for
life.
Water molecules are polar (bipolar or dipolar) due to slight negative
charge on O which is more electronegative than H which has a slight
positive charge.
Water molecules are held together by hydrogen bonding.
Water has a high latent heat of vaporisation. Evaporation of water
helps to remove heat from the body of living organisms.
Water has high specific heat capacity therefore high amount of energy
is required to increase the temperature of water.
This enables water to act as thermal buffer to create a constant internal
environment in body of living organisms.
Water is an universal solvent for ionic and polar substances and act as
medium for biochemical reactions required for the survival of living
organisms.
Water has high surface tension which is due to cohesive forces among
water molecules allows small organisms to walk on water surface.
Water has a maximum density at 4C and ice has lower density
compared to liquid water and hence aquatic organisms are able to
survive under floating ice which acts as an insulator.
Water has a low viscosity as blood plasma and lymph flow easily and
water can functions as lubricants in body joints.
Water has high boiling point and a lot of energy is required to convert
liquid water into water vapour.
Water has a high latent heat of fusion so a large amount of energy
needed to be transferred from water for it to freeze, so water is liquid
over wide range of temperatures.
This enables water to provide support by buoyancy to aquatic
organisms.
Water has high cohesive force due to hydrogen bonds among water
molecules and this helps the movement of water and mineral ions up
the xylem vessels.

BIOLOGY STPM SEMESTER 1

2. Describe with examples, three functions of carbohydrates in higher form of

animals.
Glucose: As source of energy
Glycogen in muscles or liver: As energy store
Ribose/ Deoxyribose: As component in nucleotide/ nucleic acids
Glycoproteins (Carbohydrates+ Proteins): As component in the
membrane
3. Describe with examples, three functions of carbohydrates in plants.
Glucose: As source of energy
Starch/ Glycogen: As energy store
Cellulose: As component of cell wall
Ribose/ Deoxyribose: As component in nucleotide/ nucleic acids
Glycoprotein: As component in membrane
4. Explain the differences between disaccharides and polysaccharides.
Disaccharides

Polysaccharides

Soluble in water

Insoluble in water

Taste sweet

Do not taste sweet

Can be crystallised

Cannot be crystallised

Has reducing properties except

sucrose

Has no reducing properties

Made up of two monosaccharides

Made up of many monosaccharides

Not branched

Can be branched or unbranched

Examples include maltose, lactose

and sucrose.

Examples include cellulose, starch

and glycogen

BIOLOGY STPM SEMESTER 1

5. Explain how the molecular structures of cellulose are related to its functions.
Cellulose plays a structural role in plants.
Made up of long chain of -glucose linked by -1,4-glycosidic bonds
in which each molecule is rotated 180 with respect to adjacent
molecules in the chain.
Unbranched linear cellulose chains run parallel to each other.
Has cross linkage which is the hydrogen bond that gives stability and
strength
A group of cellulose chains forms a microfibril which are then
arranged in large bundles to give tremendous tensile strength.
Fibres laid in layers in different directions adding further strength.
Insoluble in water.
6. Describe two functions of cellulose.
Forms cell wall and can prevent cells from rupturing when cells are
turgid.
Fully permeable to water and solutes to allow movement of substances
in and out of cells.
7. With reference of cellulose, explain briefly the term polymerisation. State
briefly the differences between the formation of polysaccharides and
polypeptides.
Polymerisation is formation of long repeated units of monomers (or
basic units) by condensation with the removal of water molecules.
In cellulose, the monomer is -glucose, which linked together by 1,4-glycosidic bonds.
Polysaccharides

Polypeptides

Does not involve ribosome

Involve ribosome

Only involve one type of

monomer which is -glucose

Involve 20 different types of

amino acids

Formation of glycosidic bonds

between the molecules

Formation of peptide bond

between the monomers

Does not involve genes/DNA

Involve genes/ DNA to code the

amino acids sequence

Does not involve mRNA and

tRNA

Involve mRNA and tRNA

Does not involve transcription and

translation

Involves transcription and

translation

BIOLOGY STPM SEMESTER 1

8. Explain how the molecular structures of starch are related to its functions.
Starch functions as storage compound in plants.
It is a mixture of amylose and amylopectin.
Amylose is an unbranched chain of -glucose linked by -1,4glycosidic bonds in the form of helix.
Amylopectin is a branched chains of -glucose linked by -1,4glycosidic bonds and -1,6-glycosidic bonds and also in the form of
helix.
Compound stabilised by countless hydrogen bonds.
Compact and insoluble.
Readily hydrolysed to form sugar when required.
9. An example of polysaccharides playing a storage role in animals glycogen
Glycogen has similar structure as amylopectin but it has more
branching.
Glycogen is a branched chain of -glucose linked by -1,4-glycosidic
bonds and -1,6-glycosidic bonds and also in the form of helix.
Advantages for organisms in storing polysaccharides such as glycogen,
rather than storing glucose.
Glycogen is insoluble in water
Glycogen has no effect on the osmotic pressure in cell
It is a compact molecule made from many units of glucose and
hence can store more energy
Can be easily hydrolysed into glucose for cellular respiration
when needed
10. Describe briefly the primary, secondary, tertiary and quaternary structures of
proteins. State the importance of these structures which are related to the
properties of protein.
Primary structure refers to the sequence of amino acids joined by
peptide bonds in a polypeptide chain.
Secondary structure
Regular pattern of coiled or folded poplypeptide chain
Maintained by hydrogen bonds between CO-group of one
amino acid and NH-group of another.
Alpha-helix formed from coiling of a polypeptide chain.
Beta-pleated sheet formed from folding of a polypeptide chain.
Fibrous proteins which are insoluble in water consist of
proteins of secondary structures.
Fibrous proteins perform structural function for examples,
keratin in hair and nails, collagen in tendon.

BIOLOGY STPM SEMESTER 1

Tertiary Structure
Refer to specific and precise three dimensional compact
structure formed from folding and coiling of polypeptide chain.
With interaction between R groups/ side chains.
Maintained by hydrogen bonds, disulphide bonds and
hydrophobic interactions.
o Disulfide bond is between cysteine amino acids.
o Hydrogen bond is between polar groups amino acids
o Ionic bond is between ionised amino group and ionised
carboxyl group
o Hydrophobic interaction is between non polar side
chains
Is globular with spherical shape
Soluble in water with hydrophilic / polar groups facing to
outside
Tertiary structure is important for the functions of soluble
proteins such as enzymes, hormones and antibodies.

Quaternary Structure
Formed from the association of more than one polypeptide
chains.
Haemoglobin is an example of globular protein having
quaternary structure
Haemoglobin is made up of four polypeptide chains held
together by
o Disulfide bond is between cysteine amino acids
o Hydrogen bond is between polar groups
o Ionic bond is between ionised amino acids and ionised
carboxyl groups
o Hydrophobic interaction is between non-polar side
chains
Each polypeptide chain of haemoglobin has a haem group or
prosthetic group containing iron atom for binding to oxygen
molecules.
Collagen is an example of fibrous protein having quaternary
structure
In collagen, there are 3 polypeptides in the form of helix
maintained by hydrogen bonds
Adjacent collagen molecules are linked by covalent bonds

11. What is meant by protein denaturation?

Protein denaturation occurs when bonds that maintain specific secondary,
tertiary or quaternary structure of the protein are broken resulting in loss of
specific 3 dimensional structure and loss of function of the protein.

BIOLOGY STPM SEMESTER 1

12. Explain three factors which may cause protein denaturation.

Increase of temperature beyond optimum temperature causes
denaturation of protein as ionic bond, hydrogen bond and hydrophobic
interaction that maintain the specific secondary, tertiary and quaternary
structure of protein are broken due to high kinetic energy at higher
temperature.
Changes in pH occurs in which strong acids or alkalis are added,
excess hydrogen ions or excess hydroxyl ions which alters the charges
of protein break the hydrogen/ ionic bonds in the protein to cause
denaturation
Heavy metal ions such as mercury denature proteins by breaking ionic
bonds
Organic solvent break hydrophobic interaction
13. The function and structures of proteins ae related. Discuss the statement in
relation to globular protein.
Globular proteins are soluble and often involved in chemical reaction
Examples of globular proteins include haemoglobin, enzymes,
hormones and antibodies.
A globular protein refers to a specific and precise three dimensional
compact structure formed from folding and coiling of polypeptide
chain with interaction between R groups / side chains.
The tertiary structure is held in shape by 4 types of bonds between R
groups : hydrogen bonds, ionic bonds, disulphide bonds, hydrophobic
or Van der Waals interactions.
Globular proteins are soluble because the R groups on the outer
surfaces are hydrophilic and can form hydrogen bonds with water
Hydrophobic R groups are arranged on the inside of the molecules
Chemical bonds between R groups break and tertiary structure unfolds.
Hydrophobic R groups are then exposed so the proteins solubility is
reduced.

BIOLOGY STPM SEMESTER 1

14. Proteins can be divided into two groups namely fibrous proteins and globular
proteins, based on the shape of the molecule. Describe the differences between
the two types of proteins.
Fibrous Proteins

Globular Proteins

Do not have a tertiary structure but

have a secondary structure

Have a tertiary structure (Quaternary

may or may not be present)

Polypeptide chains are cross-linked at

interval to form long fibers

Polypeptide chain is tightly folded to

form a spherical shape

Insoluble in water, due to large

number of hydrophobic groups

Dissolve in water due to the

hydrophilic groups

Perform structural function

Perform metabolic function

Examples: Keratin, collagen, silk

Examples: Any named enzyme/ any

named protein hormones/ Antibodies
or Haemoglobin

15. What are conjugated proteins? Give examples of these proteins.

Conjugated proteins are made up of protein and non-protein
component known as a prosthetic group.
Glycoproteins are proteins that contain carbohydrates.
Glycoproteins are components of the cell membrane and form mucus
in the digestive tract
Lipoproteins are proteins that contain lipids.
Lipoproteins are components of cell membrane and plasma
lipoproteins function primarily in the transport of lipids.
Nucleoprotein are proteins that contain nucleic acids
Examples include ribosome and chromosomes
Metalloproteins are proteins that contain metal ions
Examples include haemoglobin and myoglobin

BIOLOGY STPM SEMESTER 1

16. Describe functions of lipids.

As an energy store
One gram of fat contains twice the amount of energy as one
gram of carbohydrates
Storing of fat reduces space and weight compared to stroring
carbohydrate of the same amount of energy

Formation of cell membrane

Phospholipids are components of cell membrane
Cholesterol regulate fluidity of cell membrane

As heat insulator
Adipose/ fat tissues found under the skin can act as heat
insulator

To protect internal organs

Fat tissues surround internal organs provide support and
mechanical protection

As a waterproof substance for example in the form of wax

As a precursor of other steroids as all steroids are synthesised from
cholesterols

17. Describe the properties of triglyceride

Hydrophobic/ non-polar
Less dense compared to water
Dissolve in alcohol
Many C-H bonds
Higher proportion of hydrogen to oxygen compared to carbohydrates
Lower proportion of oxygen to carbon compared to carbohydrates
Higher energy values (or energy per unit mass) compared to
carbohydrates

BIOLOGY STPM SEMESTER 1

18. State the differences between the saturated fatty acids (stearic acid) and
unsaturated fatty acid (oleic acid)
Saturated fatty acids like stearic acid have the maximum number of
hydrogen atoms and all the carbons are saturated with covalently
bound hydrogen.
All the carbons in a saturated fatty acid linked by single covalent bonds
A saturated fatty acid is a straight molecule
Triglycerides formed from saturated fatty acids are usually solid at
room temperature
Unsaturated fatty acid like oleic acid contain one or more double bonds
between carbon atoms
An unsaturated fatty acids is a bent molecule due to kinks where
double bonds are located
Triglycerides formed from unsaturated fatty acid are usually liquid at
room temperature
19. Major function of triglyceride molecule is act as energy stores as they have a
higher calorific value then carbohydrates. Explain.
Triglycerides have a higher proportion of hydrogen and much less
proportion of oxygen compared to carbohydrates.
Triglycerides have higher number of carbon to hydrogen bonds
compared to carbohydrates
Carbohydrates have numerous carbon to hydroxyl bonds
Triglycerides can provide more energy per gram on oxidation
compared to carbohydrates
20. Describe the differences between essential fatty acids and non-essential fatty
acids
Essential fatty acids such as linoleic acid cannot be synthesised by the
body and must be obtained in diet
Non-essential fatty acids can be synthesised by the body
21. Describe the esterification process
Esterification involves condensation reaction between one molecule of
glycerol and three molecules of fatty acids
Three ester bonds are formed to produce a molecule of triglyceride and
three molecules of water

BIOLOGY STPM SEMESTER 1

22. Explain the structure and characteristics of phospholipids in relation to their

roles in the membrane structure.
23. Explain why lecithin molecules are the most suitable material for cell
membrane?
Lecithin is a type of phospholipid molecule
It is formed from condensation of one molecule of glycerol with two
fatty acids and a phosphate group attached with choline
Lecithin consists of a hydrophilic head which is attracted to water and
two hydrophobic tails which are not attracted to water
The cell membrane is made up of two phospholipid layers with the
hydrophilic heads on the outside of the bilayer attracted to water and
form hydrogen bonds with water molecules
The hydrophobic tails face each other in centre of bilayer forming the
hydrophobic core and are bonded by non-polar bonding
The phospholipid bilayer forms a boundary separating the cell contents
from the external environment
Cell membrane is a matrix for the attachment of proteins
Being hydrophobic, it is selectively permeable and regulates the
movement of substances across the membrane
Substances which are lipid-soluble can cross the membrane
easily through phospholipid bilayer
Substances which are large, polar or ionic pass through with the
help of specific proteins
24. Describe the function of steroids.
A steroid is a complex organic compound with four rings of carbon
atoms interconnected to form the main skeleton and side chains of
variable length
Function of steroids
Cholesterol is a component of the cell membrane and acts to
regulate the fluidity of the membrane
Cholesterol is the precursor of other steroids such as vitamin D,
oestrogen, testosterone, progesterone, aldosterone, cortisol and
bile acids
Bile acids helps in emulsification of fats in the intestines
Cortisol functions in regulating glucose balance in the body
Aldosterone functions in maintain balance of salts in body fluid
Sex hormones such as oestrogen and testosterone regulate
reproductive activities
Vitamin D facilitates the absorption of calcium ions from the
small intestines

BIOLOGY STPM SEMESTER 1

25. Describe briefly the structure of the DNA molecules

DNA consists of two antiparallel polynucleotide strands
Both polynucleotide strands twist around each other to form a double
helix stabilised by hydrogen bonds
Each nucleotide is bonded to two other nucleotides in the same
polynucleotide strand with phosphodiester bonds.
Nucleotide bases in one polynucleotide strand form base pairs with
nucleotide bases in the other polynucleotide strand
Purine base of one polynucleotide strand wlll always base pair with
pyrimidine base of another polynucleotide strand
A will always base pair with T and G will always base pair with C
There are two hydrogen bonds between A and T and three hydrogen
bonds between G and C.
A complete turn of the DNA helix consists of 10 base pairs with a
distance of 3.4nm
26. Explain the significance of the base pairings to the structure of DNA
Complementary base pairing hold the two polynucleotide strands
together because of many hydrogen bonds
Hydrogen bonds give stability as strands not easily separated and
contributed to three dimensional structure of DNA molecule
Hydrogen bonds only form specific bases so few mistakes during
DNA replication
27. mRNA
mRNA is a linear single strand polynucleotide
mRNA is formed during transcription where the part of DNA which
codes for the specific polypeptides and known as gene or cistron is
transcribed into sequence of ribonucleotides
In eukaryotic cells, mRNA is processed to remove introns (non-coding
sequences) before it leaves the nucleus to bind to ribosome for
synthesis of polypeptide
28. rRNA
rRNA is synthesised in nucleolus and is one of the structural
component of ribosome
29. tRNA
tRNA molecules are folded to form a cloverleaf arrangement held by
hydrogen bonds between complementary bases
each tRNA has an anticodon which is complementary to the mRNA
codon for amino acid which is carried on the 3 end of the tRNA
molecule

BIOLOGY STPM SEMESTER 1

tRNA functions to carry specific amino acids to the ribosomes for

synthesis of polypeptide chain

30. State the differences between DNA and RNA

RNA
Formed by only one polynucleotide
strand

DNA
Formed by two polynucleotide
strands

Not a double helix but a straight chain Double helix

Its pentose sugar unit is ribose

Its pentose sugar unit is deoxyribose

Its bases are adenine, cytosine,

guanine and uracil

Its bases are adenine, cytosine,

guanine and thymine

A short molecule

A long molecule

There are three different typesmRNA, tRNA and rRNA

There is only one type

No complementary bases pairings by

hydrogen bonds except in tRNA

Complementary bases pairing by

hydrogen bonds between the two
strands of DNA molecules

Ratio of A+G to C+U varies

Ratio of A+G C+T

31. Paper Chromatography

Paper chromatography is a technique for separating mixtures of protein
or photosynthetic pigments into individual components which can then
be isolated for further investigation
The mixture is dissolved in a suitable solvent (or mobile phase) and are
allowed to pass over s stationery phase : a chromatography paper
Movement of molecules depends on:
Molecular size
Solubility of molecules
Adhesion of molecules to the chromatography paper
Molecules in the mixture can be identified by Rf (retardation factor)
which is constant for the same solvent used

=

2 dimensional paper chromatography is carried out as the
chromatography paper is rotated 90 and separation is repeated using
the same or different solvent