POSSIBLE QUESTIONS + SHORT ANSWERS

Cells structure
The microscope in cell

 Q.) Make preparations of cellular material suitable for viewing with a light microscope

 Q.) How to draw cells from microscope slides and photomicrographs?

Ans.) https://www.youtube.com/watch?v=VQCj1UK4zyY&list=WL&index=4

https://www.youtube.com/watch?v=ZKIILH3Qimw&list=WL&index=3

https://www.youtube.com/watch?v=VIcOVgpGxBg&list=WL&index=2

 Q.) Calculate magnifications of images and actual sizes of specimens from drawings,
photomicrographs and electron micrographs (scanning and transmission)
Ans.)https://www.youtube.com/watch?
v=5poLVpIwhBQ&list=PLvoozFtQoIVN0e7SBnIrf9t_iyC81sT7G&index=14

 Q.)Use an eyepiece graticule and stage micrometer scale to make measurements and use the
appropriate units, millimeter (mm), micrometer (µm) and nanometer (nm)
Ans.) Unit conversion Basic knowledge:
m ------ cm = x100
Cm ------ mm = x10 , mm------cm = /10
µm ------ cm = /10000
µm ------ mm = /1000 , mm ---- µm = x1000
nm ------ µm = /1000

 Q.) Define resolution and magnification and explain the differences between these terms,
with reference to light microscopy and electron
 Ans.) Magnification: Magnification is the ability to make small objects seem larger, such as
making a microscopic organism visible.
Resolution: Resolution is the ability to distinguish two objects from each other.

Cells as the basic units of living

 Q.) Recognize organelles and other cell structures found in eukaryotic cells and outline their
structures and functions:
• Cell surface membrane
Function:
-to be a barrier keeping the constituents of the cell in and unwanted substances out --
to be a gate allowing transport into the cell of essential nutrients and movement from
the cell of waste products.

Structure:
-7nm thin

-Made up of
phospholipids and
proteins

-is trilayered/ trilaminar

appearance

• nucleus:
Function:
-control activity of the cell
- store the cell's DNA, maintain its integrity, and facilitate its transcription and
replication.
Structure:
-6 µm in size
-Largest organelle in Animal cell
-it is surrounded by nuclear envelope (made up of two membranes hence it is a
double membranous organelle)
-contains nuclear pores which allow movement of substances in and out of nucleus
-the liquid inside nucleus is nucleoplasm
 -thread like structures chromatin threads are present. Chromatin fibers are coiled and
condensed to form chromosomes. The DNA is surrounded by a histone protein to
maintain shape thus making a chromatin thread.
-Substances that enter nucleus= ATP, Hormones, Nucleotides
-Substances that leave nucleus= mRNA, tRNA, ribosomes
-nucleolus number varies in cells. It is made up of loops of DNA and RNA. It makes
ribosomes from its own DNA.

• rough endoplasmic reticulum:

-Produces proteins for the rest of the cell to function. The rough endoplasmic
reticulum has on it ribosomes, which are small, round organelles whose function it is
to make those proteins.
-Transport and modification of protein (not protein synthesis!)
-is an extension of outer membrane of nucleus

• smooth endoplasmic reticulum:

• - The smooth endoplasmic reticulum functions in many metabolic processes.
It synthesizes lipids, phospholipids as in plasma membranes, cholesterol,
reproductive hormones and steroids. Cells that secrete these products, such as cells of
the testes, ovaries, and skin oil glands, have an excess of smooth endoplasmic
reticulum.
-does not have ribosomes

• Golgi body (Golgi apparatus or Golgi complex):

-is a stack of flattened sacs which packages proteins into membrane-bound vesicles
inside the cell before the vesicles are sent to their destination
-the proteins are modified in Golgi body
-the vesicles are called Golgi vesicles. If it contains hydrolytic enzymes, the vesicle is
knows as lysosomes and is slightly larger in size

https://www.youtube.com/watch?v=6UqtgH_Zy1Y

• Ribosomes :
-20nm (70S), 25nm (80S)
 -A ribosome is an intercellular structure made of both RNA and protein, and it is the
site of protein synthesis in the cell.
-The ribosome reads the messenger RNA (mRNA) sequence and translates that
genetic code into a specified string of amino acids, which grow into long chains that
fold to form proteins. (more detail on it in further chapters)
-It is made up of 2 subunits; larger and smaller
-there are two types 70S and 80S. 70S is present in both eukaryotes and prokaryotes.
80S is present only in eukaryotes.

• Mitochondria:
- 0.5-1 µm
-Double membranous organelle that generate most of the chemical energy needed to
power the cell's biochemical reactions. Chemical energy produced by the
mitochondria is stored in a small molecule called adenosine triphosphate (ATP).
-outer membrane is folded = Cristae
- The liquid present in mit= Matrix
-The space between outer and inner membrane = intermembranous space
-stalked particles: they help in the formation of ATP during aerobic respiration. The
enzyme ATP Synthase joins ADP+P = ATP. They are attached to the Cristae and are
9nm in size.

-70S ribosomes, enzymes, loops of DNA and mRNA are present. They make proteins
for aerobic respiration.
https://www.youtube.com/watch?v=i1dAnpSFbyI
 • Centrioles and microtubules
- Microtubules are major components of the cytoskeleton. They are found in all
eukaryotic cells, and they are involved in mitosis, , intracellular transport, and
maintenance of cell shape. Microtubules are composed of alpha- and beta-tubulin
subunits assembled into linear protofilaments.
THESE ARE THE
STALKED - Centrioles are paired barrel-shaped organelles located in the
PARTICALS
cytoplasm of animal cells near the nuclear envelope. Centrioles
play a role in organizing microtubules that serve as the cell's skeletal system. They
help determine the locations of the nucleus and other organelles within the cell
https://www.youtube.com/watch?v=Cu6JmQC5_bY
https://www.youtube.com/watch?v=-qV__tYb4c4
https://www.youtube.com/watch?v=oIrnecBfHzg
https://www.youtube.com/watch?v=4XmLuUa1d44

• Cilia:
-Cilia and flagella are cell organelles that are structurally similar but different in
length and function. Cilia are present in organisms such as paramecium, while
flagella can be found in bacteria and sperm cells. Cilia are shorter and more
numerous than flagella.
-Cilia and flagella are the most common organelles for locomotion in unicellular
organisms. Organisms with cilia can move faster and more efficiently.
• Microvilli:
- Microvilli are finger-like membrane protrusions, supported by the actin
cytoskeleton
- increase the surface area of the cell exposed to the lumen to enhance absorption and
secretion.
• Chloroplasts:
- 3 --- 10 µm
-double membranous organelle
- Chloroplasts are chlorophyll-containing organelles in plant cells; they play a vital
role for life on Earth since photosynthesis takes place in chloroplasts.
- Liquid part in membrane envelope= Stroma
-A system of membranes are in the Stroma. Some of them make flattened, fluid filled
sacs= thylakoids.
-Chloroplast contains photosynthetic pigments e.g. Chlorophyll. These pigments are
present in the thylakoids and grana (stacked-up thylakoids). Light dependent stage
occurs in thylakoid membranes and grana.
-In the Stroma, 70S ribosomes, loops of DNA, mRNA, enzymes are present. Light
independent stage occurs in Stroma. It also contains lipid droplets + starch grains

• Cell wall:
 - A cell wall is a structural layer surrounding some types of cells, just outside the cell
membrane. It can be tough, flexible, and sometimes rigid. It provides the cell with
both structural support and protection, and also acts as a filtering mechanism.
-In plants= made up of cellulose (fiber) , pectin, hemicellulose (these aren’t fibres but
they act as glue to hold fibres together)
Pectin + hemicellulose + cellulose = Cell Wall
In fungi= chitin
-Primary cell wall= when new cell is formed, the first cell wall made. They are rigid.
The fibers are arranged parallel. Another layer of these fibres are arranged ontop to
form a crisscross look
-Cellulosic fibres are inelastic so they have high tensile strength so cell doesn’t burst
when it is turgid.
- Some cell walls have extra deposition of cellulose giving them strength. Some have
lignin which also makes it strong and flexible.

• Plasmodesmata:
- Plasmodesmata are intercellular pores connecting adjacent plant cells allowing
membrane and cytoplasmic continuity.

• large permanent vacuole and tonoplast of plant cells :

- A vacuole is a membrane-bound cell organelle. In animal cells, vacuoles are
generally small and help sequester waste products. In plant cells, vacuoles help
maintain water balance. 
- Tonoplast: a membrane which bounds the chief vacuole of the cell
Functions=
 -the sap is highly concentrated so water moves in hence cell becomes turgid.
Provides support.
-may have hydrolytic enzymes which helps in hydrolysis
-contain chemicals aka secondary metabolites. These are not essential for growth but
they contribute; e.g. pigments
-certain alkaloids and tannins are present which prevent animals eating them.
-food reserves like sugars, proteins.
-vacuole is important for increasing volume

 Q.) Describe and interpret photomicrographs, electron micrographs and drawings of typical
plant and animal cells
 Q.) Compare the structure of typical plant and animal cells
 Q.) What is ATP used for in living cells?
Ans.) Cells use ATP from respiration for energy-requiring processes

 Q.) Outline key structural features of a prokaryotic cell as found in a typical bacterium
Ans.)
• unicellular
• generally 1–5 µm diameter
• peptidoglycan cell walls
• circular DNA
• 70S ribosomes
• absence of organelles surrounded by double membranes

 Q.) Compare the structure of a prokaryotic cell as found in a typical bacterium with the
structures of typical eukaryotic cells in plants and animals
Ans.) Bacterium features: Cell wall, cell membrane, cytoplasm, ribosomes, plasmid,
flagellum, Pilli, DNA (loosely suspended), foldings.

 Q.) State the features of viruses.

Ans.) All viruses are non-cellular structures with a nucleic acid core (either DNA or RNA)
and have a capsid made of protein. Some viruses have an outer envelope made of
phospholipids. They can crystalize when conditions are too extreme.
 Biological molecules
Testing for biological molecules
 Q.) Describe and carry out the Benedict’s test for reducing sugars, the iodine test for starch,
the emulsion test for lipids and the biuret test for proteins

Ans.) Benedict’s test for reducing sugars:

-monosaccharaides
1. The sample which is to be tested is added to a clean test tube. (vol is mentioned)
2. An equal volume of Benedict’s reagent (copper II sulfate) is added. (vol is
mentioned)
3. The solution is heated at 80C - 90C for 3-5 mins (mentioned in que)
4. If reducing sugars are present, they will reduce the Cu2+ ions in copper II sulfate to
Cu+ ions, forming orange red precipitate.

The iodine test for starch

-sample is prepared according to questions requirements
1) sample is placed in clean test tube
2) Potassium iodide solution / Iodine solution is added to the test tube via dropper
3) Gently shake the test tube.
4) Start recording time
5) If starch is present, the solution changes colour from red-brown to blue-black.
Emulsion test for lipids:
1. The sample prepared is added to a clean test tube
2. Ethanol is added to the test tube and the solution is mixed thoroughly to dissolve any
lipid.
3. Water is then added to tube and mixed gently
4. If lipids are present, a cloudy white substance appears / sol goes cloudy

-this is because lipids are hydrophobic so they “come out of” the solution and forms
an emulsion.

Biuret Test for Proteins:

1. Sample is added to clean test tube
2. Sodium Hydroxide/Biuret A is then added
3. A few drops of Copper II Sulphate/Biuret B is added
4. Gently shake
5. If protein is present, the colour of reagent changes from blue to purple
 6.

 Q.) Describe and carry out a semi-quantitative Benedict’s test on a reducing sugar solution by
standardizing the test and using the results (time to first color change or comparison to color
standards) to estimate the concentration

 Q.) Describe and carry out a test to identify the presence of non-reducing sugars, using acid
hydrolysis and Benedict’s solution
1. Ans.) Take a sample in the test tube.
2. Add Hydrochloric acid to the sample
 3. The test tube is heated in a water bath of boiling 80C-100C for 3-5 mins
This results in the hydrolysis of the non-reducing disaccharide into 2
monosaccharaides – these are reducing sugars
4. The sample is then neutralized with Sodium Hydrogencarbonate solution
5. Now the sample can be tested using the usual benedict’s test
6. If colour changes now, then non-reducing sugars were present in the original sample.

Carbohydrates and lipids

 Q.) Describe and draw the ring forms of α-glucose and β-glucose

α- glucose:
-It is an isomer of D-glucose having a hydroxyl group located downward. It has a low
melting point and high stability. Alpha glucose has a hydroxyl group on 1 position, on the
same side, as the hydroxyl group of position 4.
β- glucose:
-Beta glucose is an isomer of (D) glucose having a hydroxyl group on 1 position, on the
opposite side, as the hydroxyl group of position 4. An example of a polymer having beta
glucose monomers is cellulose. It has a high melting point and more stability

-The glucose has two isomers, alpha glucose and beta glucose. The main difference between
the two lies in the orientation of the (-OH) hydroxyl group. In both cases, the hydroxyl group
gets connected to the first carbon atom, just the geometry is different.
  Q.) Define the terms monomer, polymer, macromolecule, monosaccharide, disaccharide and
polysaccharide
Ans.) Monomer: Monomers are atoms or small molecules that bond together to
form more complex structures such as polymers.
 Q.) State the role of covalent bonds in joining smaller molecules together to form polymers
 Q.) State that glucose, fructose and maltose are reducing sugars and that sucrose is a non-
reducing sugar
 Q.) Describe the formation of a glycosidic bond by condensation, with reference to
disaccharides, including sucrose, and polysaccharides
 Q.) Describe the breakage of a glycosidic bond in polysaccharides and disaccharides by
hydrolysis, with reference to the non-reducing sugar test
 Q.) Describe the molecular structure of the polysaccharides starch (amylose and amylopectin)
and glycogen and relate their structures to their functions in living organisms
 Q.) Describe the molecular structure of the polysaccharide cellulose and outline how the
arrangement of cellulose molecules contributes to the function of plant cell walls
 Q.) State that triglycerides are non-polar hydrophobic molecules and describe the molecular
structure of triglycerides with reference to fatty acids (saturated and unsaturated), glycerol
and the formation of ester bonds
 Q.) Relate the molecular structure of triglycerides to their functions in living organisms
 Q.) Describe the molecular structure of phospholipids with reference to their hydrophilic
(polar) phosphate heads and hydrophobic (non-polar) fatty acid tails

2.3 Proteins

 Q.) Describe and draw the general structure of an amino acid and the formation and breakage
of a peptide bond
  Q.) Explain the meaning of the terms primary structure, secondary structure, tertiary structure
and quaternary structure of proteins
 Q.) Describe the types of interaction that hold protein molecules in shape:
 hydrophobic interactions
 hydrogen bonding
 ionic bonding
 covalent bonding, including disulfide bonds
 Q.) State that globular proteins are generally soluble and have physiological roles and fibrous
proteins are generally insoluble and have structural roles
 Q.) Describe the structure of a molecule of hemoglobin as an example of a globular protein,
including the formation of its quaternary structure from two alpha (α) chains (α–globin), two
beta (β) chains (β–globin) and a haem group
 Q.) Relate the structure of haemoglobin to its function, including the importance of iron in
the haem group
 Q.) Describe the structure of a molecule of collagen as an example of a fibrous protein, and
the arrangement of collagen molecules to form collagen fibres 8 relate the structures of
collagen molecules and collagen fibres to their

2.4 Water

 Q.) Explain how hydrogen bonding occurs between water molecules and relate the properties
of water to its roles in living organisms, limited to solvent action, high specific heat capacity
and latent heat of vaporization

Enzymes
Mode of action of enzymes

 Q.) state that enzymes are globular proteins that catalyse reactions inside cells (intracellular
enzymes) or are secreted to catalyse reactions outside cells (extracellular enzymes)
 Q.) explain the mode of action of enzymes in terms of an active site, enzyme–substrate
complex, lowering of activation energy and enzyme specificity, including the lock-and-key
hypothesis and the induced-fit hypothesis
  Q.) investigate the progress of enzyme-catalysed reactions by measuring rates of formation of
products using catalase and rates of disappearance of substrate using amylase
 Q.) outline the use of a colorimeter for measuring the progress of enzyme-catalysed reactions
that involve color changes

Factors that affect enzyme action

 Q.) investigate and explain the effects of the following factors on the rate of enzyme-
catalysed reactions:
 temperature
 pH (using buffer solutions)
 enzyme concentration
 substrate concentration
 inhibitor concentration
 Q.) explain that the maximum rate of reaction (Vmax) is used to derive the Michaelis–
Menten constant (Km), which is used to compare the affinity of different enzymes for their
substrates
 Q.) explain the effects of reversible inhibitors, both competitive and non-competitive, on
enzyme activity
 Q.) investigate the difference in activity between an enzyme immobilised in alginate and the
same enzyme free in solution, and state the advantages of using immobilised enzymes

Cell membranes and transport

Fluid mosaic membranes

 Q.) describe the fluid mosaic model of membrane structure with reference to the hydrophobic and
hydrophilic interactions that account for the formation of the phospholipid bilayer and the
arrangement of proteins
 Q.) describe the arrangement of cholesterol, glycolipids and glycoproteins in cell surface
membranes
 Q.) describe the roles of phospholipids, cholesterol, glycolipids, proteins and glycoproteins in cell
surface membranes, with reference to stability, fluidity, permeability, transport (carrier proteins
 and channel proteins), cell signaling (cell surface receptors) and cell recognition (cell surface
antigen)
 Q.) outline the main stages in the process of cell signaling leading to specific responses:
• secretion of specific chemicals (ligands) from cells
• transport of ligands to target cells
• binding of ligands to cell surface receptors on target cells

4.2 Movement into and out of cells

• Q.) 1 describe and explain the processes of simple diffusion, facilitated diffusion,
osmosis, active transport, endocytosis and exocytosis
• Q.) investigate simple diffusion and osmosis using plant tissue and non-living materials,
including dialysis (Visking) tubing and agar
• Q.) illustrate the principle that surface area to volume ratios decrease with increasing size
by calculating surface areas and volumes of simple 3-D shapes (as shown in the
Mathematical requirements)
• Q.) investigate the effect of changing surface area to volume ratio on diffusion using agar
blocks of different sizes
• Q.) investigate the effects of immersing plant tissues in solutions of different water
potentials, using the results to estimate the water potential of the tissues
• Q.) explain the movement of water between cells and solutions in terms of water
potential and explain the different effects of the movement of water on plant cells and
animal cells

Nucleic acids and protein synthesis

Structure of nucleic acids and replication of DNA

• Q.) describe the structure of nucleotides, including the phosphorylated nucleotide ATP
(structural formulae are not expected)
• Q.) state that the bases adenine and guanine are purines with a double ring structure, and
that the bases cytosine, thymine and uracil are pyrimidines with a single ring structure
(structural formulae for bases are not expected)
• Q.) describe the structure of a DNA molecule as a double helix, including:
• the importance of complementary base pairing between the 5′ to 3′ strand and the 3′ to 5′
strand (antiparallel strands)
• differences in hydrogen bonding between C–G and A–T base pairs
• linking of nucleotides by phosphodiester bonds 4 describe the semi-conservative
replication of DNA during the S phase of the cell cycle, including:
• the roles of DNA polymerase and DNA ligase (knowledge of other enzymes in DNA
replication in cells and different types of DNA polymerase is not expected)
• the differences between leading strand and lagging strand replication as a consequence of
DNA polymerase adding nucleotides only in a 5′ to 3′ direction 5 describe the structure of
an RNA molecule, using the example of messenger RNA (mRNA)

Protein synthesis
• Q.) state that a polypeptide is coded for by a gene and that a gene is a sequence of
nucleotides that forms part of a DNA molecule
• Q.) describe the principle of the universal genetic code in which different triplets of DNA
bases either code for specific amino acids or correspond to start and stop codons
• Q.) describe how the information in DNA is used during transcription and translation to
construct polypeptides, including the roles of:
• • RNA polymerase
• • messenger RNA (mRNA)
• • codons
• • transfer RNA (tRNA)
• • anticodons
• • ribosomes
• Q.) state that the strand of a DNA molecule that is used in transcription is called the
transcribed or template strand and that the other strand is called the non-transcribed
strand
• Q.) explain that, in eukaryotes, the RNA molecule formed following transcription
(primary transcript) is modified by the removal of non-coding sequences (introns) and the
joining together of coding sequences (exons) to form mRNA
• Q.) state that a gene mutation is a change in the sequence of base pairs in a DNA
molecule that may result in an altered polypeptide
• Q.) explain that a gene mutation is a result of substitution or deletion or insertion of
nucleotides in DNA and outline how each of these types of mutation may affect the
polypeptide produced