Chapter2 :Molecular

Biology
Pages (63-130)
2.1 Molecules to metabolism – living organisms control their
composition by a complex web of chemical reactions.
PAGE 63
• Today, molecular biology is focused on explaining the range of living
processes in terms of the chemical substances involved.

• about 99% of living matter consists of just four elements: carbon,

hydrogen, oxygen and nitrogen.

• Why do these four elements predominate in living things?

2.1 Molecules to metabolism
PAGE 63
• The elements carbon, hydrogen and oxygen make up the greater part
of us because :
1. living things contain large quantities of water.
2. most other molecules present in cells and organisms are
compounds of carbon combined with hydrogen and oxygen,
including the carbohydrates, lipids and nucleic acids.
Compounds containing carbon and hydrogen are known as organic
compounds
The carbon atom, how it forms stable compounds, and its
significance
PAGE no 64
• Carbon can be used to make a huge range of different molecules.
• This has given living organisms almost limitless possibilities for the
chemical composition and activities of their cells. The diversity of
carbon compounds is explained by the properties of carbon.
The carbon atom, how it forms stable compounds, and its
significance
PAGE no 64
 Carbon properties
page 64

• Carbon atoms form covalent bonds with other atoms.

• A covalent bond is formed when two adjacent atoms share a pair of electrons, with one
electron contributed by each atom.
• Covalent bonds are the strongest type of bond between atoms so stable molecules based on
carbon can be produced.
• Each carbon atom can form up to four covalent bonds – more than most other atoms, so
molecules containing carbon can have complex structures.
• The bonds can be with other carbon atoms to make rings or chains of any length.
• The bonds can also be with other elements such as hydrogen, oxygen, nitrogen or phosphorus.
• Carbon atoms can bond with just one other element, such as hydrogen in methane, or they can
bond to more than one other element as in ethanol (alcohol found in beer and wine).
• The four bonds can all be single covalent bonds or there can be two single and one double
covalent bond, for example in the carboxyl group of ethanoic acid (the acid in vinegar).
The carbon atom, how it forms stable compounds, and its
significance
PAGE no 64
 Classifying Carbon Compounds
• Life is based on carbon compounds including :
*carbohydrates, *lipids, *proteins and *nucleic acids.

• They have different properties and so can be used for different purposes.
• Carbohydrates are characterized by their composition.
• They are composed of carbon, hydrogen and oxygen, with hydrogen and
oxygen in the ratio of two hydrogen atoms to one oxygen, hence the
name carbohydrate
 Classifying Carbon Compounds
• Lipids are a broad class of molecules that are:
insoluble in water, including:
*Steroids, *waxes, *fatty acids and *triglycerides.
In common language, triglycerides :
are fats if they are solid at room temperature or oils if they are liquid at
room temperature.
 Classifying Carbon Compounds
• Proteins are composed of one or more chains of amino acids.
• All of the amino acids in these chains contain the elements carbon, hydrogen,
oxygen and nitrogen, but two of the twenty amino acids also contain sulphur.

• Nucleic acids are chains of subunits called nucleotides, which contain carbon,
hydrogen, oxygen, nitrogen and phosphorus.
• There are two types of nucleic acid: ribonucleic acid (RNA) and
deoxyribonucleic acid (DNA).
Drawing molecules
 What is metabolism ?
Page no 66
• Metabolism is the web of all the enzyme catalysed reactions in a cell
or organism.
• All living organisms carry out large numbers of different chemical
reactions.
• These reactions are catalysed by enzymes.
• Most of them happen in the cytoplasm of cells but some are
extracellular, such as the reactions used to digest food in the small
intestine.
• Metabolism is the sum of all reactions that occur in an organism.
What is
metabolism ?
Page no 66

• Metabolism consists of
pathways by which one type of
molecule is transformed into
another, in a series of small
steps.
• These pathways are mostly
chains of reactions but there are
also some cycles
What is metabolism ?
Page no 66
 What is metabolism?
Anabolism :endergonic reactions
page 66

• Anabolism is the synthesis of complex

molecules from simpler molecules including
the formation of macromolecules from
monomers by condensation reactions.

• Anabolism includes these processes:

1. Protein synthesis using ribosomes.
2. DNA synthesis during replication.
3. Photosynthesis, including production of
glucose from carbon dioxide and water.
4. Synthesis of complex carbohydrates
including starch, cellulose and glycogen
 What is metabolism?
Catabolism : exergonic reaction

• Catabolism is the breakdown of complex molecules into simpler

molecules including the hydrolysis of macromolecules into monomers.
• Catabolic reactions release energy and in some cases this energy is
captured in the form of ATP, which can then be used in the cell.
• Catabolism includes these processes:
1. Digestion of food in the mouth, stomach and small intestine.
2. Cell respiration in which glucose or lipids are oxidized to carbon dioxide
and water.
3. Digestion of complex carbon compounds in dead organic matter by
decomposers.
Falsification of theories
■ Molecular biology, metabolism and ‘vitalism’
• It was once believed that organic compounds could be produced only
by the chemical processes within living things.
• The view was that a vital force or ‘spark’ in life created the molecules
of living matter – the chemicals of life could not be reproduced by
‘test-tube’ reactions.
• This theory was known as ‘vitalism’
 Falsification of theories
■ Molecular biology, metabolism and ‘vitalism’
• Frederick Wöhler heated ammonium cyanate, an inorganic compound, and
produced urea.

• Urea is a typical animal product – produced by the liver Wöhler had

synthesized biological material from non-biological substances.
• The results of his demonstration – once they were widely accepted – ended the
idea of vital force. Today, molecular biology explains living processes in terms of
the chemical substances involved, without controversy.
Hydrogen bonding in water:
Water molecules are polar and hydrogen
bonds form between them.
Page 82
 Properties of water :
Cohesive, Surface tension ,Adhesive, Thermal and Solvent properties of water.
Page
1. Cohesive properties:
Cohesion refers to the binding together of two
molecules of the same type, for instance two
water molecules.
Water molecules are cohesive – they cohere,
which means they stick to each other, due to
hydrogen bonding.
This property is useful for water transport in
plants.
Water is sucked through xylem vessels at low
pressure.
Due to hydrogen bonding water can be pulled
up to the top of the tallest trees – over a
hundred metres.
 Properties of water :
Cohesive, Surface tension ,Adhesive, Thermal and Solvent properties of water.
Page
• Related to the property of cohesion is the
property of surface tension.
• The outermost molecules of water form
hydrogen bonds with the water molecules
below them.
• This gives water a very high surface tension –
higher than any other liquid except mercury.
• The surface tension of water is exploited by
insects that ‘surface skate’ .
• The insect’s waxy cuticle prevents wetting of its
body, and the mass of the insect is not great
enough to break the surface tension.
• Below the surface, water molecules slide past
each other very easily. This property is
described as low viscosity.
• Consequently, water flows readily through
narrow capillaries, and tiny gaps and pores.
 Properties of water :
cohesive, adhesive, thermal and solvent properties of water.
Page

• Adhesive properties :
• Adhesion is the force by which individual molecules cling to surrounding
material and surfaces.
Hydrogen bonds can form between water and other polar molecules, causing
water to stick to them. This is called adhesion.
This property is useful in leaves, where water adheres to cellulose molecules in
cell walls.
If water evaporates from the cell walls and is lost from the leaf via the network
of air spaces, adhesive forces cause water to be drawn out of the nearest xylem
vessel. This keeps the walls moist so they can absorb carbon dioxide needed for
photosynthesis.
Properties of water :
cohesive, adhesive, thermal and solvent properties of water.
Page

• Thermal properties of water:

1. High specific heat capacity.
2.High latent heat of vaporization.
3. High latent heat of fusion.
4. High boiling point.
 Solvent properties of water:

• Water is a powerful solvent for polar

substances such as:
1. ionic substances like sodium chloride (Na+
and Cl– ); all cations (positively charged ions) and
anions (negatively charged ions) become
surrounded by a shell of orientated water
molecules.

2. carbon-containing (organic) molecules with

ionized groups (such as the carboxyl group –
COO– and amino group –NH3 +); soluble organic
molecules like sugars dissolve in water due to the
formation of hydrogen bonds with their slightly
charged hydroxyl groups (–OH).
Transport of metabolites in the blood – and their solubilities in water
•comparing water and
methane Comparison of the
thermal properties of water
with those of methane.
2.3 Carbohydrates and lipids – compounds of carbon,
hydrogen and oxygen are used to supply and store energy.
Page 87
• Carbohydrates are:
1. The largest group of organic compounds found in living things.
2. They include sugars, cellulose, starch and glycogen.
3. Carbohydrates are compounds that contain only three elements:
carbon, hydrogen and oxygen, with hydrogen and oxygen always
present in the ratio 2:1.
2.3 Carbohydrates and lipids – compounds of carbon, hydrogen
and oxygen are used to supply and store energy.
Page 87
• Three types of carbohydrates commonly found in living things.
1. Monosaccharides (one sugar)
Glucose, galactose, Fructose, Ribose, Deoxyribose
2. Disaccharides (two sugars)
Maltose, Lactose, Sucrose.
3. Polysaccharides (many sugars)
Starch, cellulose, glycogen, chitin.
2.3 Carbohydrates and lipids – compounds of carbon, hydrogen
and oxygen are used to supply and store energy.
Page 87
Monosaccharides
page 88
• Monosaccharides are carbohydrates with relatively small molecules.
They taste sweet and are soluble in water.
• In biology, glucose is an especially important monosaccharide
because:
• all green leaves manufacture glucose using light energy.
• our bodies transport glucose in the blood
• all cells use glucose in respiration – we call it one of the respiratory
substrates
• in cells and organisms, glucose is the building block for very many
larger molecules
Monosaccharides
page 88
Test for ‘reducing sugars’
page 90
• This reaction is used to test for
reducing sugar(glucose, fructose)
and is known as Benedict’s test
• If no reducing sugar is present, the
solution remains blue.
• The colour change observed
depends on the concentration of
reducing sugar. The greater the
concentration, the more
precipitate is formed and the
greater the colour change: blue →
green → yellow → red → brown
Test for ‘reducing sugars’
page 90
Test for ‘reducing sugars’
page 90
 Test for ‘reducing sugars’
page 90
• All monosaccharides are reducing sugars. Glucose, fructose, and
galactose are monosaccharides and are all reducing sugars. 
• Is maltose a reducing sugar? Yes.
• Is lactose a reducing sugar? Yes.
•  Maltose (glucose + glucose) and lactose (galactose + glucose) have
a free aldehyde group and thus are reducing sugars. 
• Is sucrose a reducing sugar? No. Sucrose (glucose + fructose) lacks a
free aldehyde or ketone group and therefore is non-reducing.
Disaccharides
• Disaccharides are
carbohydrates made of
two monosaccharides
combined together.
• Formed by
condensation reactions
Polysaccharides: ‘Poly’ means many and, in fact,
thousands of ‘saccharide’ residues make up a polysaccharide.
• Built from very many monosaccharide residues condensed together.
• Each residue is linked by a glycosidic bond.
• So a polysaccharide is an example of a giant molecule, a
macromolecule.
• Normally, each polysaccharide contains only one type of monomer.
Cellulose is a good example – built from the monomer glucose.
Polysaccharides: ‘Poly’ means many and, in fact, thousands of
‘saccharide’ residues make up a polysaccharide.
Page 91
• Starch, glycogen and cellulose are all made by linking together
glucose molecules, yet their structure and functions are very
different.
• This is due to differences in the type of glucose used to make them
and in the type of linkage between glucose molecules.
Polysaccharides: ‘Poly’ means many and, in fact, thousands of
‘saccharide’ residues make up a polysaccharide.
Page 91
Polysaccharides: ‘Poly’ means many and, in fact,
thousands of ‘saccharide’ residues make up a polysaccharide.
Page 91
• Cellulose make fibres that are straight and uncoiled.
• When they are extracted from plants, cellulose fibres have many
industrial uses.
• We use cellulose fibres as cotton, we manufacture them into paper,
rayon fibres for clothes manufacture, nitrocelluose for explosives,
cellulose acetate for fibres of multiple uses, and cellophane for
packaging.
• Cellulose is a polymer of β-glucose molecules combined together by
glycosidic bonds between carbon-4 of one β-glucose molecule and
carbon-1 of the next.
 Polysaccharides.

• Starch is the major storage carbohydrate of most plants. It is laid down as compact
grains in plastids called leucoplasts.

• Starch is an important energy source in the diet of many animals, too. Its
usefulness lies in the compactness and insolubility of its molecule. Also, it is
readily hydrolysed to form sugar when required.
• We sometimes see ‘soluble starch’ as an ingredient of manufactured foods. Here
the starch molecules have been broken down into short lengths, making them
more easily dissolved.
• We test for starch by adding a solution of iodine in potassium iodide. Iodine
molecules fit neatly into the centre of the starch helix, creating a blue–black colour.
Polysaccharides.
• Starch is made by linking together α-glucose molecules.
• As in cellulose, the links are made by condensation reactions between
the OH groups on carbon atom 1 of one glucose and carbon atom 4 of
the adjacent glucose.
• These OH groups both point downwards, so all the glucose molecules in
starch can be orientated in the same way.
• The consequence of this is that the starch molecule is curved, rather than
straight.
• There are two forms of starch. In amylose the chain of α-glucose
molecules is unbranched and forms a helix. In amylopectin the chain is
branched, so has a more globular shape
Polysaccharides.
 Polysaccharides.
• Glycogen
is very similar to the branched form of starch, but there is more branching,
making the molecule more compact.
Glycogen is made by animals and also some fungi.
It is stored in the liver and some muscles in humans.
Glycogen has the same function as starch in plants: it acts as a store of
energy in the form of glucose, in cells where large stores of dissolved
glucose would cause osmotic problems.
https://www.iitianacademy.com/ib-dp-biology-slhl-question-bank/

• Question 1 /paper 2
• Nitrogen is part of many important substances in living organisms.
• Draw labelled diagrams to show a condensation reaction between two amino acids.
Answer Q1 /paper 2
Question 2/paper 2
 Lipids/ general characteristics
page 94
1. Contain the elements carbon, hydrogen and oxygen, as do
carbohydrates, but in lipids the proportion of oxygen is much less.
2. are present as animal fats and plant oils, and also as the phospholipids
of cell membranes.
3. Fats and oils their only difference is that at about 20ºC (room
temperature) oils are liquid and fats are solid.
4. Lipids are insoluble in water. In fact, they generally behave as ‘water-
hating’ molecules, a property described as hydrophobic.
5. lipids can be dissolved in organic solvents, such as alcohol (e.g. ethanol)
and propanone (acetone).
Fats and oils are triglycerides.
Page 94
• Fats and oils are compounds called triglycerides.
• A triglyceride is made by combining three fatty acids with one glycerol

• Each of the fatty acids is linked to the glycerol by a condensation

reaction, so three water molecules are produced.

• The linkage formed between each fatty acid and the glycerol is an
ester bond.
Fats and oils are triglycerides.
Page 94
Phospholipid:
• A phospholipid has a similar chemical structure
to triglyceride; here, one of the fatty acid groups
is replaced by phosphate .
• This phosphate is ionized and is, therefore, water
soluble.
• So phospholipids combine the hydrophobic
properties of the hydrocarbon tails with
hydrophilic properties of the phosphate.
• Phospholipid molecules form monolayers and
bilayers in water
• A phospholipid bilayer is a major component of
the plasma membrane of cells.
 Cholesterol
• The lipid cholesterol is a component of the
diet, particularly when animal fats are
present.
• This lipid, a steroid, is of different chemical
structure from that of the fatty acids.
• The ‘skeleton’ of a steroid is a set of
complex rings of carbon atoms; the bulk of
the molecule is hydrophobic, but the polar
–OH group is hydrophilic.
Fatty acids Page 95
• fatty acids combined in a triglyceride may vary in their
length (hydrocarbon chain ).

• Fatty acids can be saturated, monounsaturated or

polyunsaturated.
Unsaturated fatty acids: can be cis or trans isomers.
Page 98
• In unsaturated fatty acids in living
organisms:
• If the hydrogen atoms are nearly
always on the same side of the two
carbon atoms that are double
bonded – these are called cis-fatty
acids.
• If the hydrogens to be on opposite
sides – called trans-fatty acids.
Unsaturated fatty acids: can be cis or trans isomers.
Page 98
Unsaturated fatty acids: can be cis or trans isomers.
Page 98
• The cis and trans fats are significant because:
• our enzymes can ‘recognize’ the difference between cis and trans
forms of molecules at their active sites .
• enzymes of lipid metabolism generally recognize and can trigger
metabolism of the cis forms, but not the trans forms
• diets rich in trans fats increase the risk of coronary heart disease by
raising the levels of LDL cholesterol in the blood and lowering the
levels of HDL cholesterol
The roles of fats and oils as energy store and metabolic water source.
Page 98
Body mass index(BMI)

• Determination of body mass index by :

1. calculation

2. use of nomogram.
BMI can also be found using a type of chart called a
nomogram. A straight line between the height on the
left hand scale and the mass on the right hand scale
intersects the BMI on the central scale.
BMI
Data –Based Questions:
Nomograms and BMI

• Use the figure below to answer these questions:

1 a) State the body mass index of a man who has a
mass of 75 kg and a height of 1.45 metres.

b) Deduce the body mass status of this man.

Data –Based Questions:
Nomograms and BMI
2 a) A woman has a height of 150 cm and a BMI of
40. Calculate the minimum amount of body mass
she must lose to reach normal body mass status.
Show all of your working.

3 b) Suggest two ways in which the woman could

reduce her body mass.
Health consequences of the lipid content of diets.
Page 98
• Check your book .
Atherosclerosis and coronary thrombosis are together known as
coronary heart disease (CHD).

Many research has been done to try to identify factors that increase
the risk of CHD. The following factors all increase the statistical risk:
Increasing age
Being male rather than female
Having a family history of CHD

A person’s lifestyle can also introduce factors that increase the

risk of CHD:
Obesity
Physical inactivity
High blood pressure
Tobacco smoking
 2.4 Proteins – proteins have a very wide range of functions in living organisms.
Page 102

1. Proteins make up about two-thirds of the total dry mass of a cell.

2. They differ from carbohydrates and lipids in that they contain the element
nitrogen and, usually, the element sulfur, as well as carbon, hydrogen and
oxygen.
3. Amino acids are the molecules from which peptides and proteins are built –
typically several hundred or even thousands of amino acid molecules are
combined together to form a protein.
4. Notice that the terms ‘polypeptide’ and ‘protein’ can be used interchangeably
but, when a polypeptide is about 50 amino acid residues long, it is generally
agreed to have become a protein.
Amino acids – the
building blocks of
peptides
Peptide linkages
page 103
• Two amino acids combine
together with the loss of water to
form a dipeptide.
• This is one more example of a
condensation reaction.

• The *amino group of one amino

acid reacts with the* carboxyl
group of the other, forming a
peptide linkage (Figure 2.31).
Peptide linkages
page 103
• Proteins differ in :
1. the variety of amino acids
2. number of amino acids
3. order of their constituent amino acids.

The order of amino acids in the polypeptide chain is controlled by the

coded instructions stored in the DNA of the chromosomes in the
nucleus (page 110).
Changing one amino acid in the sequence of a protein may alter its
properties completely.
 The structure of proteins
page 104
• Once the chain is constructed, a protein takes up a specific shape.

• Shape matters with proteins – their shape is closely related to their function. This is
especially the case in proteins that are enzymes.

• The four levels of structure to a protein are shown in Table 2.6.

• When a protein loses its three-dimensional shape, we say it has been denatured.

• Heat or a small deviation in pH from the optimum can have the effect of
denaturation.
https://youtu.be/hok2hyED9go
• There are many biotechnological uses for proteins
including enzymes for removing stains,
monoclonal antibodies for pregnancy tests or
insulin for treating diabetics.
• Pharmaceutical companies now produce many
different proteins for treating diseases. These tend
to be very expensive, as it is still not easy to
synthesize proteins artificially.

• Increasingly, genetically modified organisms are

being used as microscopic protein factories.
Every individual has a unique proteome
page 105
• Most, but not all, organisms assemble their proteins from the same amino acids, but
the proteins of each individual organism are unique.
• The proteome is the entire set of proteins expressed by the genome of the
individual organism.
• It is because the genome, the whole of the genetic information of an organism, is
unique to each individual that the proteome it causes to be expressed is also unique.
• Proteomics is the study of the structure and function of the entire set of proteins of
organisms.
• The word is derived from ‘protein’ and ‘genome’, and the study is made possible, in
part, by the capacity of modern computers.
• Today, the industrial production of proteins by microorganisms (including of
genetically modified ones), when cultured in fermenters, is a source of protein for
the food, pharmaceutical, and other industries
Discovery of the role of DNA as information
molecule
Discovery of the role of DNA as information
molecule
 Genes and ‘nonsense’ DNA sequences

• The Human Genome Project (page 135) has established that the three
million bases of our chromosomes represent far fewer genes than was
originally expected.
• In fact, protein-coding sequences of our DNA account for only
approximately 1.5%. The remainder include some DNA sequences that
regulate the expression of protein-coding genes (regulatory DNA
sequences), but that leaves 70% of our DNA with other roles or none.
(At one time these regions were described as ‘junk’ or ‘nonsense’ DNA’).
Genes and ‘nonsense’
DNA sequences

• In fact, these extensive ‘non-gene’ regions of

eukaryotic chromosomes also consist of:
 introns: These are non-coding nucleotide
sequences, one or more of which interrupts
the coding sequences (exons) of eukaryotic
genes .
• Exons are expressed!
• Introns are intruders that must be removed.
 • Telomeres: These are special nucleotide sequences, typically
Genes and consisting of multiple repetitions of one short nucleotide sequence.
‘nonsense’ DNA They occur near the ends of DNA molecules and ‘seal’ the DNA ends
of the linear DNA. Here, they stop erosion of the genes that would
sequences occur with each repeated round of replication
Genes and ‘nonsense’ DNA sequences
genes for transfer RNA (tRNA):
• These are parts of the DNA template that code for relatively short lengths of
RNA that are formed in the nucleus and pass out into the cytosol.
• Here they transfer amino acids from the pool there, to supply a growing
polypeptide in a ribosome.
major lengths of non-coding DNA. Today, these are important to genetic
engineers, for they are exploited in DNA profiling. They are short sequences
of bases that are repeated very many times. Where they often occur
together in major clusters, they are known as ‘variable number tandems
repeat’ regions (VNTRs). Their use in genetic fingerprinting (DNA profiling) is
described in Chapter 3 (page 176).
Replication – DNA copying itself
• A copy of each chromosome must pass into daughter cells formed by
cell division, so the chromosomes must first be copied (replicated).
Replication –
DNA copying
itself
Replication – DNA copying itself
https://youtu.be/TNKWgcFPHqw
Enzymes involved in DNA replication are:

• Helicase (unwinds the DNA double helix)

• Gyrase/Topoisomerase (relieves the buildup of torque during
unwinding)
• Primase (lays down RNA primers)
• DNA polymerase III (main DNA synthesis enzyme)
• DNA polymerase I (replaces RNA primers with DNA)
• Ligase (fills in the gaps)
Enzymes involved in DNA replication.
2.7 DNA replication, transcription and translation – genetic
information in DNA can be accurately copied and can be translated to
make the proteins needed by the cell
• A copy of each chromosome must pass into daughter cells formed by
cell division, so the chromosomes must first be copied (replicated).

• Remember, this process takes place in the interphase nucleus, well

before the events of nuclear division.
 DNA replication steps:

1. The first step in replication is the ‘unzipping’ of the two strands. An enzyme called helicase unwinds the DNA
double helix at one region, breaks the hydrogen bonds there that hold the strands together and then
temporarily keeps the strands of the helix separated.
• The unpaired nucleotides are now exposed, surrounded by a pool of free-floating nucleotides.
2. In the next step, both strands of DNA act as templates in replication. Complementary nucleotides line up
opposite each base of the exposed strands – adenine pairs with thymine, cytosine with guanine.

3. Hydrogen bonds then form between the complementary bases, holding them in place.
4. Finally, a condensation reaction links the sugar and phosphate groups of adjacent nucleotides, so forming
the new strands.

This reaction is catalysed by an enzyme called DNA polymerase. The enzyme has a ‘proof-reading’ role in
replication, too – any mistakes that start to happen (such as the wrong bases attempting to pair up) are
corrected.
The result is that the two strands formed are identical to the original strands. DNA replication is
DNA replication steps:
DNA replication steps:
 The evidence for semi-
conservative DNA replication.
• Experimental evidence that DNA replication is semi-conservative came
from an experiment by Meselson and Stahl.
• In the first step, they grew a culture of the bacterium E. coli in a medium
(food source) where the available nitrogen contained only the heavy
nitrogen isotope, 15N.
• Consequently, the DNA of the bacterium became entirely ‘heavy’.
• These bacteria were then transferred to a medium of the normal (light)
isotope, 14N. New DNA manufactured by the cells was now made of
14N.
• The change in concentration of 15N and 14N in the DNA of succeeding
generations was measured.
• The DNA was extracted from samples of the bacteria from each
succeeding generation and the DNA in each sample was separated.
• This was done by placing the sample on top of a salt solution of
increasing density, in a centrifuge tube.
• Thus, DNA with ‘heavy’ nitrogen ended up nearer the base of the tubes,
whereas DNA with ‘light’ nitrogen stayed near the top of the tubes.
 The evidence for semi-
conservative DNA replication.
https://youtu.be/yDQg7uXShUs
Protein synthesis:
https://youtu.be/gG7uCskUOrA
• We have seen that proteins are linear series of amino acids condensed together.
• Most proteins contain several hundred amino acid residues, but all are built from only 20
different amino acids.
• The unique properties of a protein lie in:
1. which amino acids are involved in its construction
2. the sequence in which these amino acids are condensed together.
3. The number of amino acids residues.
The sequence of bases in DNA dictates the order in which specific
amino acids are assembled and combined together.
Protein synthesis:
• All proteins are formed in the cytoplasm, some at free-floating
ribosomes, and others at the ribosomes on RER.
• For this to happen, a mobile copy of the information in the genes has
to be made, and then transported to these sites of protein synthesis.
• That copy is made of RNA and is called messenger RNA (mRNA). It is
formed by a process called transcription.
• So both DNA and RNA have roles in protein synthesis.
What are the main steps in protein synthesis?
• Transcription – the first step in protein synthesis.
• In Stage 2 of protein synthesis, the amino acids of the pool available
for protein synthesis are activated by combining with short lengths of
a different sort of RNA, transfer RNA (tRNA).
• Translation – the last step in protein synthesis