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S.5 Chemicals of Life 2025 BY AKORA

The document outlines the importance of chemicals of life, particularly focusing on water and its properties, roles, and interactions with both polar and non-polar substances. It emphasizes water's unique characteristics, such as being a universal solvent, and its critical functions in biological systems. Additionally, it discusses the role of minerals and ions in biological processes, highlighting their significance in cellular structures and metabolic functions.
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0% found this document useful (0 votes)
53 views34 pages

S.5 Chemicals of Life 2025 BY AKORA

The document outlines the importance of chemicals of life, particularly focusing on water and its properties, roles, and interactions with both polar and non-polar substances. It emphasizes water's unique characteristics, such as being a universal solvent, and its critical functions in biological systems. Additionally, it discusses the role of minerals and ions in biological processes, highlighting their significance in cellular structures and metabolic functions.
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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CHEMICALS OF LIFE NOTES S.

5 2025 BY AKORA KENNETH

THE NEW ADVANCED SECONDARY CURRICULUM

CLASS: S.5

TOPIC: CELL BIOLOGY

SUB TOPIC 1: CHEMICALS OF LIFE

Competency: The learner evaluates cells and tissues, by analysing and relating their structure

to function, as a basis for medical research in order to improve health.

LEARNING OUTCOMES

The learner should be able to:

Analyse the properties and functions of chemical compounds (water, lipids, proteins including enzymes from
mammals) in a cell, focusing on their roles in maintaining cellular structure and metabolic processes in living
organisms. (Thermal properties of water not required.)

CHEMICALS OF LIFE

These are compounds needed to maintain life of living organisms. They are divided into two groups, i.e.

i) Inorganic compounds e.g. water, vitamins, salts, acids and roughages.


ii) Organic compounds e.g. carbohydrates, lipids, proteins and nucleic acids.

WATER

It is the most important inorganic compound in life and most abundant within living organism.

A human cell contains about 80% water and the whole body has over 60% water.

Water is formed when two hydrogen atoms combine with an oxygen atom by sharing electrons. The shape of a water
molecule is triangular and the angle between the nuclei of atoms is approximately 105 DEGREES

Water molecules form weak hydrogen bonds with other water molecules nearby and its bonds give it the unique
properties.

Properties of water
i) It is liquid at room temperature.
ii) It has a high heat capacity therefore much energy is used to raise its temperature because it is used to
break the hydrogen bonds which restrict the mobility of the molecules. As a result water is relatively slow
to heat up or to cool down thus a high heat capacity.
iii) Water expands as it freezes unlike other liquids which contract on cooling.
iv) Water reaches its maximum density above its freezing point at 4 oC hence when water freezes, the ice
formed is less dense than the water and hence floats on top of the surface. In this way, ice insulates water
below making it less dense and able to float hence the water will be warmer than the air above.
v) Water has a high surface tension. Surface tension is the force that causes the surface of a liquid to
contract so that it occupies the least area. It is high due to the fact that molecules are oriented so that most
hydrogen bonds point inwards towards other water molecules.
vi) It has a high latent heat of fusion i.e. much heat must be removed before freezing occurs.
vii) It has high adhesive and cohesive properties preventing it from breaking under tension.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

viii) It is colourless and transparent.


ix) It has a low viscosity i.e. water molecules slide over each other very easily.
x) It dissolves more substances than any other liquid i.e. it is a universal solvent.
Functions of water
➢ It is a component of cells
➢ It is a solvent and a medium of transport
➢ It is a reagent in hydrolysis
➢ It enables fertilization by swimming gametes
➢ It enables dispersal of seeds, fruits, gametes and larvae stages in aquatic organisms.
➢ It is important in transpiration in plants.
➢ It is important in translocation in plants.
➢ It enables germination to proceed by activating enzymes, transporting hydrolyzed stored food, swelling and
breaking open the testa.
➢ It is involved in Osmo-regulation in animals
➢ It enables cooling by evaporation as a result of sweating and panting.
➢ It is a component of lubricants at joints e.g. the synovial fluid.

➢ It offers support in hydrostatic skeleton.


➢ It offers protection as a component of mucus and tears.
➢ It enables migration to occur as a result of river flow or ocean currents.
QUESTION: HOW DO THE PROPERTIES OF WATER RELATE TO ITS BIOLOGICAL ROLE?
1) Water is transparent and this allows light penetration in aquatic habitats to enable photosynthesis of aquatic
autotrophs and visibility of aquatic animals.
2) Water has a low viscosity and this allows for smooth flow of water and other dissolved substances in an aquatic
medium for easy transport.
3) It has a high surface tension providing support to aquatic organisms and allowing movement of living organisms on
water surface.
4) Has a high latent heat of vaporization hence a cooling effect on the body surface since evaporation of water from
the body of an organism draws out excess heat.
5) It has a high boiling point thus provides a stable habitat and medium since a lot of heat which is not normally
provided in the natural environment is needed to boil the water.
6) It has a high latent heat of fusion and hence a low freezing point thus providing a wide range of temperature for
survival of aquatic organisms since it prevents freezing of cells and cellular components.
7) It has a high specific heat capacity which minimizes drastic temperature changes in biological systems and
provides a constant external environment for many plant cells and aquatic organisms.
8) It has a maximum density at 4o C hence ice floats on top of water insulating the water below hence increasing the
chances of survival of aquatic organisms below the ice.
9) Water is liquid at room temperature providing a liquid medium for living organisms and metabolic reactions and a
medium of transport.
10) It has high adhesive and cohesive forces creating enough capillarity forces for transport in narrow tubes of
biological systems.
11) It is a universal solvent hence providing a medium for biochemical reactions.
12) Water is a polar molecule allowing solubility of polar substances, ionization or dissociation of biochemical
substances.
13) Water is incompressible thus providing support in hydrostatic skeleton and herbaceous stems.
14) Water is neutral hence does not alter the pH of cellular components on their environment.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

15) A water molecule is relatively small for easy and fast transport across a membrane.
QUESTION: OUTLINE THE ROLE OF MINERALS AND IONS IN BIOLOGICAL SYSTEMS.
1) They are components of smaller molecules e.g. phosphorus is contained in ATP and iodine is contained in
thyroxin, etc.
2) They are constituents of large molecules e.g. proteins contain nitrogen and sulphur, phospholipids contain
phosphorus, nucleic acids contain nitrogen and phosphorus, etc.
3) They are components of pigments e.g. haemoglobin and cytochromes which contain ion, chlorophyll contain
magnesium, etc.
4) They are metabolic activators e.g. activates glucose before it is broken down in cell respiration, calcium ions
activate ATPase enzyme during muscle contraction.
5) They determine the anion, cation balance e.g. Na+ , K+ and Ca+ are important in transmission of impulses and
muscle contraction.
6) They determine the osmotic pressure and water potential so that it does not fluctuate beyond narrow limits e.g. Na+
, K+ and Cl- are involved in water balance in the kidneys.
7) They are constituents of structures in cell membranes, cell walls, bones, enamel and shells.

INTERACTION OF WATER WITH POLAR AND NON-POLAR SUBSTANCES.

The interaction of water with polar and non-polar substances is a fundamental concept in chemistry, primarily
influenced by water's molecular structure and the nature of the substances it interacts with. Water is a highly polar
molecule, meaning it has a partial positive charge on the hydrogen atoms and a partial negative charge on the oxygen
atom due to its bent shape and the difference in electronegativity between oxygen and hydrogen.

1. Interaction of Water with Polar Substances

Polar substances are molecules that have an uneven distribution of charge, resulting in a dipole moment. These
substances can interact with water through hydrogen bonding or dipole-dipole interactions.

- Hydrogen Bonding: This occurs when the partial positive charge of hydrogen in water interacts with the partial
negative charge of an electronegative atom (like oxygen or nitrogen) in the polar substance. This is the main
interaction that allows water to dissolve many polar substances, like salts (NaCl), alcohols, and sugars. For example,
in water, the hydrogen of one water molecule can form a hydrogen bond with the oxygen atom of another molecule.

- Solubility of Polar Substances: Because of these interactions, water is often referred to as the "universal solvent" for
polar compounds. Polar substances are generally soluble in water because their positive and negative poles interact
with the positive and negative parts of the water molecules. For example, NaCl (sodium chloride) dissolves in water
because the positively charged sodium ions (Na⁺) are attracted to the oxygen (partially negative) of water, while the
negatively charged chloride ions (Cl⁻) are attracted to the hydrogen (partially positive) atoms of water.

Water interacts strongly with polar substances due to its own highly polar nature. Water molecules have a bent shape
with a partial positive charge on the hydrogen atoms and a partial negative charge on the oxygen atom. This polarity
allows water to form interactions like hydrogen bonding with other polar molecules, enabling it to dissolve or
interact in a variety of ways with different polar substances.

Key Mechanisms of Interaction Between Water and Polar Substances:

1. Hydrogen Bonding
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

Hydrogen bonding is the primary force through which water interacts with polar substances. A hydrogen bond is an
attractive interaction between a hydrogen atom, which is covalently bonded to an electronegative atom (like oxygen
or nitrogen), and another electronegative atom with a lone pair of electrons. Since water has an oxygen atom with lone
pairs of electrons, it can form hydrogen bonds with polar molecules that contain electronegative atoms (such as
oxygen or nitrogen).

- Example: Water and Alcohols: Alcohols, such as ethanol (C₂H₅OH), are polar because they have a hydroxyl group (-
OH). The oxygen in the hydroxyl group can form hydrogen bonds with the hydrogen atoms of water molecules. This
is why ethanol is miscible (able to mix in all proportions) with water.

- Example: Water and Acids/Bases: Many acids and bases are polar and can dissolve in water because of their ability
to form hydrogen bonds. For instance, hydrochloric acid (HCl) dissociates in water to form H⁺ and Cl⁻ ions, and water
molecules surround and stabilize these ions through hydrogen bonding.

2. Dipole-Dipole Interactions

Besides hydrogen bonding, water can also interact with other polar molecules through dipole-dipole interactions.
These interactions occur between the positive end of one molecule and the negative end of another molecule.

- Example: Water and Acetone (C₃H₆O): Acetone, a polar solvent, contains a carbonyl group (C=O), which has a
partial negative charge on the oxygen atom and a partial positive charge on the carbon atom. Water molecules can
align their positive hydrogen atoms with the negative oxygen of acetone, forming dipole-dipole interactions. This is
why acetone is miscible with water.

3. Ion-Dipole Interactions

When polar substances dissolve in water, they can dissociate into ions (charged particles). Water can interact with
these ions through ion-dipole interactions, which occur between the charged ions and the partial charges on the water
molecules.

- Example: Water and Sodium Chloride (NaCl): Sodium chloride is an ionic compound that dissociates into Na⁺ and
Cl⁻ ions when it dissolves in water. The partially negative oxygen atoms of water molecules surround the positively
charged sodium ions (Na⁺), and the partially positive hydrogen atoms surround the negatively charged chloride ions
(Cl⁻). These ion-dipole interactions help dissolve the salt in water, making it a common example of water's ability to
dissolve polar and ionic substances.

4. Solubility of Polar Substances in Water

Water is often called the "universal solvent" because it is excellent at dissolving many polar substances. This
solubility is driven by the fact that water molecules can surround polar solutes and form favorable interactions
through hydrogen bonds, dipole-dipole, and ion-dipole interactions.

- Example: Sugar (Sucrose): Sucrose, a polar molecule, dissolves in water because the hydroxyl groups (-OH) in
sucrose can form hydrogen bonds with the water molecules. This interaction helps break the sugar's intermolecular
forces, allowing it to dissolve in water and form a homogeneous solution.

5. Formation of Hydration Shells

When a polar substance dissolves in water, the water molecules arrange themselves around the solute molecules to
maximize the interactions between the solute and the solvent. This arrangement of water molecules around the solute
is called a hydration shell.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

- Example: Dissolving Ionic Compounds: When salts like NaCl dissolve in water, the water molecules surround each
ion in a hydration shell. The oxygen atoms (with their partial negative charge) surround the cations (Na⁺), and the
hydrogen atoms (with their partial positive charge) surround the anions (Cl⁻), stabilizing the ions in solution and
preventing them from recombining into solid salt.

Examples of Polar Substances That Interact Well with Water:

1. Salts: Ionic compounds like sodium chloride (NaCl), potassium chloride (KCl), and magnesium sulfate (MgSO₄)
are polar and dissociate into ions when mixed with water, interacting through ion-dipole forces.

2. Alcohols: Organic compounds like ethanol (C₂H₅OH) and methanol (CH₃OH) are polar due to their hydroxyl (-OH)
groups, and they can form hydrogen bonds with water molecules, making them soluble in water.

3. Sugars: Carbohydrates, such as glucose (C₆H₁₂O₆), are polar due to their multiple hydroxyl groups. These molecules
can form hydrogen bonds with water, making them highly soluble in water.

4. Acids and Bases: Many acids, like hydrochloric acid (HCl), and bases, like sodium hydroxide (NaOH), are polar
and dissociate into ions when dissolved in water, leading to strong interactions with water molecules.

Conclusion:

Water’s polarity is key to its interactions with other polar substances. The formation of hydrogen bonds, dipole-dipole
interactions, and ion-dipole interactions allows water to dissolve and interact with a wide range of polar molecules.
This ability to form favorable interactions with other polar molecules underpins water's status as the "universal
solvent," making it essential for countless biological and chemical processes. Whether it’s dissolving salts, alcohols,
or sugars, water’s unique structure allows it to engage in a variety of interactions that support life and facilitate
chemical reactions.

2. Interaction of Water with Non-Polar Substances

Non-polar substances, on the other hand, lack a significant charge difference within the molecule, meaning they don't
have positive or negative poles. This leads to very different interactions with water.

- Lack of Hydrogen Bonding: Non-polar substances do not form hydrogen bonds with water because they don't have
the necessary dipole character. Water molecules, being highly polar, prefer to interact with other polar molecules or
ions, rather than with non-polar molecules.

- Formation of Hydrophobic Interactions: When non-polar substances are introduced into water, they tend to cluster
together rather than dissolve. This behavior is referred to as "hydrophobic" (water-fearing) interaction. The non-polar
molecules are unable to form favorable interactions with the polar water molecules, so the water molecules tend to
reorganize around the non-polar molecules to minimize their exposure to the non-polar substance. This leads to the
non-polar molecules aggregating together, forming structures like oil droplets in water.

- Solubility of Non-Polar Substances: Non-polar substances, such as oils, fats, and hydrocarbons, generally do not
dissolve in water. Since there is no attraction between the non-polar molecules and the water molecules, the non-polar
molecules remain separated. For example, when oil is added to water, the oil forms a separate layer instead of
dissolving because the water molecules prefer to bond with each other rather than interact with the oil molecules.

The interaction of water with non-polar substances is an interesting and important concept in chemistry, particularly
when discussing solubility, molecular interactions, and behavior in various environments.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

1. Polarity of Water

Water (H₂O) is a highly polar molecule. The oxygen atom in a water molecule has a partial negative charge, and the
hydrogen atoms have partial positive charges. This polarity gives water several unique properties, including the ability
to form hydrogen bonds and interact with other polar substances.

2. Non-Polar Substances

Non-polar substances are molecules where the charge distribution is symmetrical, meaning there is no significant
difference in electronegativity between the atoms in the molecule, resulting in no dipole moment. Examples of non-
polar substances include oils, fats, and hydrocarbons (e.g., methane, benzene, and hydrocarbons like hexane).

3. Why Non-Polar Substances Don't Mix Well with Water

Since water is polar and non-polar substances lack significant charges or dipoles, there is minimal interaction between
water molecules and non-polar molecules. Water molecules prefer to interact with other polar molecules, forming
hydrogen bonds and maintaining their own hydrogen-bonding network. When water encounters a non-polar
substance, the interactions between water and the non-polar molecules are weak and don't disrupt the water’s
hydrogen-bonded structure effectively.

Because of this, non-polar substances are generally insoluble in water. For example, if you try to mix oil and water,
the water molecules will form hydrogen bonds with each other, and the oil molecules will stick together. The two will
separate, with the non-polar oil forming its own distinct phase.

4. "Like Dissolves Like"

This principle is central in chemistry, especially when considering solubility. Since water is polar, it tends to dissolve
other polar or ionic substances (like salts or sugars), whereas non-polar solvents tend to dissolve other non-polar
substances. This is why oil (non-polar) and water (polar) do not mix.

5. Hydrophobic Effect

This term describes the tendency of non-polar substances to cluster together in water rather than interact with the
water molecules. This behavior is primarily driven by entropy. When non-polar substances are in water, the water
molecules around them become more ordered (because they form a "cage-like" structure around the non-polar
substance), which is thermodynamically unfavorable. The non-polar molecules "hide" from the water molecules to
minimize this ordering, resulting in the formation of distinct non-polar phases.

This effect plays a crucial role in biological systems, such as the formation of cell membranes, where hydrophobic
molecules like lipids form bilayers to shield their hydrophobic tails from water.

6. Interaction on Molecular Level

At the molecular level, when water encounters non-polar substances, the interactions that occur are mainly van der
Waals forces (specifically dispersion forces), which are much weaker than the hydrogen bonds that water forms with
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

itself or with polar molecules. These weak interactions don't provide the necessary energy to dissolve non-polar
substances in water.

7. Surfactants as Intermediaries

In practical situations, surfactants (molecules with both polar and non-polar regions) can help to mix water with non-
polar substances. Surfactants have a hydrophilic (water-loving) head and a hydrophobic (water-fearing) tail, allowing
them to interact with both water and non-polar substances. This is why detergents can emulsify oils (non-polar) in
water.

8. Applications

• Oil Spills: The difficulty in mixing non-polar substances like oils with water is a challenge in cleaning up oil
spills. Specialized surfactants are used to break up the oil and help it disperse.
• Biological Systems: The hydrophobic effect is fundamental to the structure and function of proteins and
cellular membranes. For example, the hydrophobic amino acids in a protein will typically fold inward, away
from the surrounding water.
• Emulsification: In food chemistry, non-polar substances like oils are mixed with water to create emulsions
(e.g., mayonnaise). This process relies on surfactants or emulsifiers to keep the oil droplets suspended in the
water phase.

Conclusion

The interaction between water and non-polar substances is minimal due to the fundamental difference in polarity. This
results in poor solubility of non-polar substances in water, leading to phenomena like phase separation and the
hydrophobic effect. However, surfactants and other agents can be used to overcome this, allowing for the mixing of
water with non-polar substances in specific applications.

3. Key Differences in Water’s Interaction with Polar and Non-Polar Substances

The interaction of water with polar and non-polar substances is governed by the fundamental differences in
molecular structure and the nature of intermolecular forces. Let’s explore the key differences in how water interacts
with these two types of substances:

1. Polarity of the Substances

• Polar Substances: Polar molecules, like water itself, have an uneven distribution of electrical charge, with
one part of the molecule being slightly negative (typically the oxygen atom) and another part being slightly
positive (typically the hydrogen atoms). This creates a dipole moment, meaning that one end of the molecule
has a partial positive charge and the other has a partial negative charge.
• Non-Polar Substances: Non-polar molecules do not have an uneven charge distribution. The electrons are
more symmetrically shared, resulting in no significant positive or negative ends (dipoles). Non-polar
molecules may be homonuclear (e.g., O₂, N₂) or heteronuclear (e.g., hydrocarbons like methane or oil), but
they lack a dipole moment.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

2. Intermolecular Forces

• With Polar Substances: Water molecules can interact strongly with polar molecules because of hydrogen
bonding. The partial positive charge of hydrogen in water can interact with the partial negative charge of
electronegative atoms (like oxygen or nitrogen) in polar molecules. This allows water to dissolve many polar
substances (like salts and sugars) through the formation of hydrogen bonds.
• With Non-Polar Substances: Water’s interaction with non-polar molecules is much weaker, primarily
relying on van der Waals forces (specifically dispersion forces). These forces are much weaker than
hydrogen bonds, and as a result, non-polar substances tend to be poorly soluble in water.

3. Solubility

• Polar Substances in Water: Water is an excellent solvent for polar substances due to the “like dissolves
like” principle. Since water is polar, it tends to dissolve other polar substances or ionic compounds (like salts)
because of the strong interactions between water molecules and the polar solutes. For instance, water can
dissolve sodium chloride (NaCl) because the positively charged sodium ions (Na⁺) and negatively charged
chloride ions (Cl⁻) interact favorably with the polar water molecules.
• Non-Polar Substances in Water: Non-polar substances do not dissolve well in water. Since water molecules
prefer to interact with other polar molecules, non-polar substances like oil, fats, and hydrocarbons do not
dissolve in water. Instead, they tend to form separate phases, like when oil forms droplets or a layer on top of
water.

4. Hydrophobic vs. Hydrophilic Effects

• Hydrophilic (Water-Loving) Substances: Polar molecules and ions that can form hydrogen bonds with
water are considered hydrophilic. They interact favorably with water, forming strong connections that result
in high solubility in water. Examples include salts, alcohols, and sugars.
• Hydrophobic (Water-Fearing) Substances: Non-polar molecules tend to be hydrophobic because they do
not form strong interactions with water. In fact, water molecules surrounding non-polar substances tend to
form an ordered structure (which is entropically unfavorable), so these substances tend to aggregate or
separate from water. This is known as the hydrophobic effect and is a driving force in the behavior of
biological molecules like proteins and lipids.

5. Structure and Behavior in Water

• Polar Molecules in Water: When polar molecules are mixed with water, they typically dissolve and
distribute evenly in the solution. Water molecules surround and stabilize the solute through hydrogen bonds.
For example, when salt (NaCl) is added to water, water molecules surround and separate the Na⁺ and Cl⁻ ions,
dissolving them.
• Non-Polar Molecules in Water: Non-polar molecules tend to form distinct separate phases or aggregates in
water. For example, when oil is added to water, it forms separate droplets or layers because the water
molecules prefer to interact with each other rather than with the oil molecules. The non-polar molecules
aggregate together to minimize the disruption of the water’s hydrogen-bonding network.

6. Effects on Biological Systems


CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

• Polar Interactions in Biology: Polar molecules are crucial in biological processes. Water’s ability to dissolve
ions and polar molecules is essential for cellular functions, like nutrient transport, enzyme activity, and signal
transduction. Hydrophilic interactions also play a significant role in the formation of hydrophilic channels in
cell membranes and the folding of proteins.
• Non-Polar Interactions in Biology: Non-polar molecules are equally important in biological systems. For
example, the hydrophobic effect drives the formation of lipid bilayers in cell membranes, where the
hydrophobic tails of lipids aggregate together, away from the water, while the hydrophilic heads face
outward, interacting with the water. Additionally, the folding of proteins into their native structures often
involves the burial of hydrophobic regions in the interior of the protein to avoid interaction with water.

7. Examples of Polar vs. Non-Polar Interactions with Water

• Polar: When sugar (sucrose) is dissolved in water, the hydroxyl (-OH) groups of sugar form hydrogen bonds
with water molecules. This is why sugar dissolves easily in water.
• Non-Polar: When hexane (a non-polar hydrocarbon) is added to water, the molecules do not interact
significantly with the water molecules. Instead, the hexane forms a separate phase, as water molecules prefer
to interact with each other rather than with the non-polar hexane molecules.

8. Energy Considerations (Enthalpy and Entropy)

• Polar Molecules: The interactions between polar substances and water are typically exothermic, meaning
they release energy as they form hydrogen bonds. This makes these interactions favorable in terms of both
enthalpy and entropy, and thus, polar molecules tend to dissolve well in water.
• Non-Polar Molecules: The lack of strong interactions between water and non-polar molecules leads to
unfavorable enthalpy changes. Furthermore, when non-polar substances are added to water, water molecules
become more ordered around the non-polar substance, leading to a decrease in entropy. This makes the
interaction energetically unfavorable, which is why non-polar substances don’t dissolve in water.

Summary of Key Differences:

Property Polar Substances Non-Polar Substances


Polarity Uneven charge distribution (dipole moment). Symmetrical charge distribution, no dipole.
Intermolecular
Hydrogen bonds (strong) and dipole-dipole. Van der Waals forces (weak).
Forces
Solubility in Water High solubility (dissolve in water). Low solubility (form separate phases).
Water forms separate phases with non-
Effect on Water Water surrounds and dissolves polar solutes.
polar solutes.
Involved in hydration, nutrient transport, and Drives the formation of cell membranes,
Biological Role
enzyme interactions. protein folding.
Example Salt (NaCl), alcohol, sugar. Oil, waxes, methane.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

In essence, polar substances readily dissolve in water due to the strong attractive forces between water molecules and
the solute, while non-polar substances have limited interaction with water and generally remain separate.

LIPIDS
These are large group of organic compounds. Like carbohydrates, they contain carbon, hydrogen and oxygen but the
proportion of oxygen is smaller than in carbohydrates hence they are more reduced than the carbohydrates.
Lipids are insoluble in water.
They are of two types i.e. fats and oils. Fats are solid at room temperature while oils are liquids at room temperature.
Properties of lipids
• They are insoluble in water but soluble in non-polar solvents like benzene, chloroform, diethyl ether, etc. The low
solubility is due to the low oxygen content which results into a small number of polar hydroxyl groups in lipids
hence very few hydrogen bonds.
• They have a high proportion of hydrogen in their molecules.
• They are non-polar compounds.
• They are less dense than water.
• They can be solids or liquids at room temperature.
• Their melting point increases with increase in saturation.
• They undergo high oxidation in respiration to yield large amounts of energy.

• They are poor conductors of heat.

SIMPLE LIPIDS

Simple lipids are a category of lipids that consist of fatty acids and alcohol, without any additional functional groups
like phosphate or carbohydrates. They are the most basic form of lipids, and they can be further categorized based on
the types of alcohols involved (usually glycerol or long-chain alcohols). Simple lipids play vital roles in energy
storage, insulation, protection, and structure within biological systems.

Types of Simple Lipids

1. Triglycerides (Triacylglycerols):
o Structure: Composed of one molecule of glycerol (a three-carbon alcohol) and three fatty acid
molecules. The fatty acids are connected to the glycerol backbone via ester bonds.

Formation of triglycerides

Lipids are made of fatty acids and glycerol. Glycerol has 3 OH groups and each combines with a separate fatty acid to
form a lipid chemically known as a triglyceride. This is a condensation reaction that leads to liberation of 3 water
molecules.

Metabolic water is formed and an ester bond is formed between the glycerol and fatty acid. Since the glycerol
possesses 3 hydroxyl groups to which 3 fatty acids attach themselves, 3 water molecules are formed. In this reaction,
the fatty acids may all be the same or different, saturated or unsaturated.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

For example

Qn

Using the structural formular below For glycerol, and molecular formula CH3(CH2)nCOOH for a fatty acid, show the
formation of a triglyceride from fatty acids and glycerol.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

o Properties:
▪ They are typically hydrophobic (water-insoluble).
▪ The physical state (solid or liquid) depends on the fatty acid composition. If they contain
saturated fatty acids, they tend to be solid at room temperature (e.g., butter, lard). If they
contain unsaturated fatty acids, they tend to be liquid (e.g., olive oil, canola oil).
▪ They are non-polar molecules, meaning they do not dissolve in water but are soluble in
organic solvents like ether and chloroform.
o Functions:
▪ Energy Storage: Triglycerides are the main form of energy storage in the body, stored in
adipose tissue. They provide a dense source of energy, as they contain more energy per gram
than carbohydrates or proteins.
▪ Insulation and Protection: Stored triglycerides in adipose tissue act as thermal insulation
to help regulate body temperature and provide mechanical protection for internal organs.
▪ Energy Source: When energy is needed, triglycerides are broken down into fatty acids and
glycerol through a process called lipolysis and can be metabolized for ATP production.
2. Waxes:
o
Structure: Waxes are esters of long-chain fatty acids and long-chain alcohols. They differ from
triglycerides by having a single fatty acid chain esterified to an alcohol (instead of three fatty acids).
o Properties:
▪ Waxes are hydrophobic and solid at room temperature due to their long fatty acid chains.
▪ They have a high melting point, which makes them useful as protective barriers.
o Functions:
▪ Waterproofing: Waxes act as water repellents and are used by many organisms for
protection against water loss. For example, the cuticle of plant leaves is coated with wax to
prevent water evaporation.
▪ Protection: Waxes form protective coatings in various organisms, such as the beeswax in
bee hives, earwax (cerumen) in humans, and the wax coating on the feathers of birds.
▪ Structural: Waxes contribute to the structural integrity of certain plant and animal organs
by creating a hard outer layer.
3. FATTY ACIDS

All occurring lipids have glycerol and therefore it is the nature of the fatty acids which determines the characteristics
of any particular lipid. All fatty acids have a carboxyl group (COOH), the reminder of the molecule being a hydro
carbon chain of varying length.

These chains may possess one or more double bond in which case it is said to be unsaturated. If it possesses no double
bonds, it is said to be saturated.

Nature of fatty acid General formula Saturated/unsaturated Occurrence


1. Butyric acid C3H7COOH Saturated Butter fat
2. Linoleic acid C17H31COOH Unsaturated Seed oil
3. Oleic acid C17H33COOH Unsaturated All fats
4. Palmitic acid C15H31COOH Saturated Animal & veg fat
5. Selotic acid C25H51COOH Saturated Wood oil
6. Arachidic acid C19H39COOH Saturated P.nut oil
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

From the table, it is seen that the hydrocarbon chains may be very long forming long tails which extend
from the glycerol molecules. These trails are hydrophobic (water repelling) which makes the lipids
insoluble in water.

Saturated and unsaturated fatty acids


In saturated fatty acids all the available bonds in carbon atoms are used and there are a maximum possible
number of hydrogen atoms. Saturated fatty acids lack double bonds in the hydrocarbon tail.
Unsaturated fatty acids do not contain the maximum number of hydrogen atoms, they have one or more
double bonds between some of the carbon atoms in the hydrocarbon chain.
Saturated fatty acids have high melting points and are therefore found in fats while in unsaturated fatty
acids, the presence of the double bonds lowers the melting point and are therefore found in oils.
Since there are many types of fatty acids but one type of glycerol, lipids (fats and oils) vary due to the fatty acids.
Essential fatty acids
These are fatty acids which cannot be synthesized by the body and must be supplied in the diet.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

Common sources of essential fatty acids are; vegetables and seed oils. A deficiency of these fatty acids
results in retarded growth, reproductive disorders and kidney failure.
Non-essential fatty acids
These are fatty acids that can be synthesized by the body from metabolism of other compounds like proteins and
carbohydrates.
How cholesterol causes arthesclerosis
Cholesterol is produced by the liver and is used as the starting point for the synthesis of other steroid
molecules. The major source of cholesterol is diet and many dairy products are rich in cholesterol or fatty
acids from which cholesterol can be synthesized. Thyroxin stimulates cholesterol production in the liver
and also increases the rate of excretion of bile. Excessive amounts of cholesterol in blood can be harmful.
It can be deposited in walls of arteries leading to arthesclerosis and increased risk of formation of a blood
clot which may block blood vessels, a condition known as thrombosis. This is often fatal if it occurs in the
coronary artery in the wall of the heart (coronary thrombosis or heart attack) or brain (cerebral thrombosis).
Although cholesterol is harmful in excess, it is essential to have some in the diet for reasons stated.
Question: explain why lipids are insoluble in water?

Lipids are insoluble in water primarily because of their hydrophobic nature. This characteristic arises from the
structure of lipids, which are predominantly composed of long, non-polar hydrocarbon chains (fatty acids) or rings
(as in steroids). Let's break down the reasons why lipids are insoluble in water:

1. Non-Polar Nature of Lipids:

• The key feature of lipids, such as fatty acids and triglycerides, is the long hydrocarbon chains (chains of
carbon atoms bonded to hydrogen atoms). These hydrocarbon chains are non-polar, meaning they do not
have a charge or dipole.
• Water, on the other hand, is a polar molecule, with a partial negative charge on the oxygen atom and partial
positive charges on the hydrogen atoms. Polar molecules tend to interact with other polar molecules through
hydrogen bonding or dipole-dipole interactions.

2. Lack of Hydrogen Bonding with Water:

• Water molecules are highly attracted to other polar molecules because they can form hydrogen bonds, which
are a type of attractive force between the hydrogen atom of one molecule and the electronegative atom (like
oxygen) of another molecule.
• Lipids, being non-polar, cannot form hydrogen bonds with water molecules, which limits their ability to
dissolve in water.

3. Hydrophobic Effect:

• When lipids are placed in water, the hydrophobic effect occurs. The non-polar hydrocarbon chains of lipids
tend to avoid interacting with the water molecules. Instead of dissolving, the lipid molecules aggregate
together to minimize their exposure to water.
• For example, in the case of phospholipids, the non-polar tails (fatty acid chains) will face inward, away from
water, while the polar heads (phosphate groups) face outward, interacting with water. This forms lipid
bilayers in biological membranes, where the hydrophobic tails are shielded from the water.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

4. Energy Considerations:

• When water molecules surround a lipid molecule, they form a structured "clathrate" or cage-like structure
around the lipid. This structure is energetically unfavorable because it requires the water molecules to
organize themselves in a way that reduces entropy (disorder).
• Lipids do not readily interact with water to "disrupt" this ordered structure, and instead, they aggregate to
minimize the disruption of water's hydrogen-bonding network.

5. Difference in Solubility:

• Solubility in a solvent depends on the ability of molecules to interact with each other. Since water molecules
are polar and lipids are non-polar, they don't mix well. Lipids are soluble in non-polar solvents (like
chloroform or ether) because these solvents do not require the disruption of water's hydrogen bonds and have
similar non-polar characteristics as the lipid molecules.

Summary:

• Lipids are insoluble in water because their long, non-polar hydrocarbon chains (or rings) cannot interact
with water molecules, which are polar. The hydrophobic nature of lipids leads to their aggregation in water
rather than dissolving, and the hydrophobic effect minimizes the exposure of their non-polar parts to water.

4. STEROIDS

These are biologically important substances in both plants and animals. The skeleton of a steroid molecule consists of
four complex rings of carbon atoms. Three of these are six sided while one is 5 sided.

The various steroids differ in the side groups attached to the carbon atoms of the skeleton. Like lipids, they contain
hydrogen atoms and oxygen atoms but do not contain any fatty acid. They have a general skeleton shown below.

Examples of steroids include;


• Cholesterol which is a component of the plasma membrane and a raw material for many other steroids like
bile acids.
• Bile acids e.g glycolic acid and taurochloric acid used in the emulsification of fats during digestion.
• Vitamin D (calciferol) which promotes phosphorous and calcium absorption and metabolism.
• Sex hormones e.g testosterone and oestrogen. Hormones from adrenal cortex i.e are referred to as
corticosteroids.

General Properties of Simple Lipids:


CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

1. Hydrophobic Nature:
o Simple lipids, including triglycerides and waxes, are hydrophobic, meaning they repel water. This is
due to the long hydrophobic hydrocarbon chains in their structure.
2. Energy-Dense:
o They are highly energy-dense molecules. Triglycerides, in particular, provide about 9 kcal/g, which
is more than twice the energy content of carbohydrates or proteins (which provide 4 kcal/g). This
makes them the most efficient storage form of energy.
3. Solubility:
o Simple lipids are not soluble in water because they lack polar groups that can interact with water
molecules. They are, however, soluble in organic solvents like ether, chloroform, and benzene.
4. Storage:
o Simple lipids are stored in specialized cells called adipocytes (fat cells) in the body. Triglycerides are
stored in adipose tissue, where they serve as long-term energy reserves.
5. Inert and Stable:
o Waxes, in particular, are chemically inert and resistant to degradation, which is why they are used as
protective coatings by various organisms.

Functions of Simple Lipids:

1. Energy Storage:
o The primary function of triglycerides is energy storage. When energy is needed, triglycerides are
broken down to release fatty acids and glycerol, which can be metabolized to produce ATP.
2. Insulation:
o In animals, particularly mammals, stored triglycerides in adipose tissue act as insulation to conserve
heat and maintain body temperature. In cold environments, fat stores help protect the body from heat
loss.
3. Protection of Organs:
o Fat tissue (mainly triglycerides) provides cushioning around vital organs, such as the kidneys, heart,
and liver, protecting them from physical shock and injury.
4. Waterproofing and Protection:
o Waxes are used by plants and animals to prevent water loss. For example, plant leaves have a waxy
coating that prevents excessive water evaporation, and animals like birds have waxy coatings on their
feathers to keep them dry and buoyant.
5. Structural Components:
o In addition to energy storage, simple lipids (especially phospholipids and triglycerides) are integral
parts of cell membranes and provide structural support. The hydrophobic properties of lipids help
form bilayers in membranes, creating barriers that separate the cell's internal environment from the
external surroundings.
6. Chemical Signaling:
o Although this is more relevant to other types of lipids like steroids, the breakdown products of
triglycerides, such as eicosanoids (derived from polyunsaturated fatty acids), also play a role in cell
signaling and inflammation.

Summary of Simple Lipids:


CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

Type of Simple
Structure Properties Functions Examples
Lipid
Hydrophobic, energy- Butter, olive oil,
Glycerol + 3 fatty Energy storage, insulation,
Triglycerides dense, water-insoluble, animal fats (lard,
acids organ protection
storage form of fat tallow)
Long-chain fatty Hydrophobic, solid at room Waterproofing, protection, Beeswax, plant
Waxes acids + long-chain temperature, high melting structural integrity in cuticle wax, earwax,
alcohols point plants/animals candle wax

In conclusion, simple lipids (triglycerides and waxes) are crucial for energy storage, insulation, and protection. They
serve as an energy reserve in animals and humans and help organisms maintain their structure, protect their bodies,
and avoid dehydration or water loss.

CONJUGATED LIPIDS

Conjugated lipids are a class of lipids that consist of fatty acids combined with other molecules, such as proteins,
carbohydrates, or phosphates, in addition to the usual components like glycerol or sphingosine. Unlike simple lipids,
which are composed only of fatty acids and alcohol, conjugated lipids have more complex structures due to the
presence of additional functional groups. These lipids play important roles in cell signaling, membrane structure, and
various metabolic processes.

Types of Conjugated Lipids

1. Phospholipids
o Structure: Phospholipids consist of a glycerol backbone, two fatty acid chains, a phosphate group,
and sometimes an additional polar group (e.g., choline, ethanolamine, or serine).
o Properties:
▪ Amphipathic: Phospholipids have both a hydrophobic tail (the fatty acid chains) and a
hydrophilic head (the phosphate group and polar group).
▪ They are essential for membrane formation, as they form lipid bilayers in cell membranes.

STRUCTURE OF A PHOSPHOLIPID
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

A phospholipid can be simply represented as:

o Functions:
▪ Cell Membrane Structure: Phospholipids are the major components of biological
membranes, forming bilayers that act as selective barriers, controlling the movement of
substances into and out of cells.
▪ Signal Transduction: Phospholipids are involved in cell signaling, particularly through
molecules like phosphatidylinositol derivatives (e.g., inositol trisphosphate).
▪ Lipid Rafts: Phospholipids help organize lipid rafts, which are microdomains in the cell
membrane that cluster proteins involved in signaling and trafficking.
2. Glycolipids
o Structure: Glycolipids consist of a glycerol or sphingosine backbone, two fatty acids, and a
carbohydrate group (such as glucose or galactose).
o Properties:
▪ Amphipathic: Like phospholipids, glycolipids have a hydrophobic tail (fatty acids) and a
hydrophilic head (carbohydrate group).
▪ These lipids are often found in the outer leaflet of the plasma membrane.
o Functions:
▪ Cell Recognition: Glycolipids play a critical role in cell-cell recognition and
communication. The carbohydrate moiety is involved in interactions between cells and their
environment, such as in the immune response.
▪ Blood Type Determination: The ABO blood group antigens are glycolipids found on the
surface of red blood cells, which are crucial for blood type compatibility.
▪ Membrane Stability: Glycolipids help stabilize the structure of the cell membrane and
influence its fluidity.
▪ Neuroprotection: In the nervous system, glycolipids like gangliosides are involved in
neuronal protection and signaling.
3. Lipoproteins
o Structure: Lipoproteins consist of lipids (such as phospholipids, cholesterol, and triglycerides)
combined with proteins. These proteins are called apolipoproteins, and they help transport lipids
through the bloodstream.
o Properties:
▪ Amphipathic: The lipid portion is hydrophobic, while the apolipoproteins are hydrophilic,
allowing the complex to be soluble in blood plasma.
o Functions:
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

▪ Lipid Transport: Lipoproteins transport lipids (triglycerides, cholesterol) through the


bloodstream to various tissues.
▪ Types of Lipoproteins:
▪ Chylomicrons: Transport dietary lipids from the intestines to other parts of the body.
▪ VLDL (Very Low-Density Lipoproteins): Carry triglycerides from the liver to
peripheral tissues.
▪ LDL (Low-Density Lipoproteins): Deliver cholesterol to cells for membrane
synthesis and hormone production.
▪ HDL (High-Density Lipoproteins): Transport cholesterol from tissues back to the
liver for excretion or recycling.
4. Sphingolipids
o Structure: Sphingolipids are based on the sphingosine backbone rather than glycerol. They contain
one fatty acid, sphingosine, and sometimes additional functional groups, such as a phosphate or
carbohydrate group.
o Properties:
▪ Amphipathic: The hydrophobic fatty acid tail and the hydrophilic head (carbohydrate or
phosphate) give sphingolipids the ability to interact with both water and lipid environments.
o Functions:
▪ Membrane Structure: Sphingolipids are important components of cell membranes,
particularly in the nervous system. They help maintain membrane stability and are involved
in signaling.
▪ Signal Transduction: Sphingolipids, such as sphingosine-1-phosphate, act as signaling
molecules in processes like cell proliferation, survival, and migration.
▪ Neuroprotective Role: Sphingolipids such as cerebrosides and gangliosides are involved in
the myelin sheath structure around neurons, essential for efficient nerve signal transmission.

General Properties of Conjugated Lipids

• Amphipathic Nature: Most conjugated lipids, such as phospholipids and glycolipids, are amphipathic (they
have both hydrophobic and hydrophilic regions), which makes them ideal for forming the bilayers of
biological membranes. This characteristic allows them to interact with both water-soluble and lipid-soluble
substances.
• Functional Diversity: Conjugated lipids play roles beyond just structural components; they are involved in
cell signaling, membrane fluidity, transport, cell recognition, and immunological responses.
• Membrane Structure: Conjugated lipids are crucial for maintaining the structural integrity and functionality
of biological membranes. They can influence membrane properties like fluidity, flexibility, and the
organization of membrane proteins.

Functions of Conjugated Lipids

1. Cell Membrane Structure:


o Phospholipids, glycolipids, and sphingolipids are integral components of cell membranes, forming
lipid bilayers that provide a semi-permeable barrier to separate the internal environment of the cell
from the external environment.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

o The hydrophobic tails of these lipids face inward, while the hydrophilic heads face outward,
interacting with the aqueous environment inside and outside the cell.
2. Signal Transduction:
o Phosphoinositides (derived from phospholipids) play a major role in cell signaling pathways,
including activation of kinases and regulation of cellular processes like growth, differentiation, and
metabolism.
o Sphingolipids, such as sphingosine-1-phosphate, serve as second messengers in signaling pathways
involved in cell growth, survival, and apoptosis.
3. Lipid Transport:
o Lipoproteins facilitate the transport of lipids through the bloodstream, ensuring that essential lipids
(such as cholesterol and triglycerides) are delivered to cells and tissues that need them.
4. Cell Recognition and Immunity:
o Glycolipids on the surface of cells are important for cell recognition, allowing cells to identify and
communicate with each other. They play critical roles in immune responses, including the recognition
of pathogens.
o Glycolipids are also involved in blood type determination (e.g., ABO blood group).
5. Neuroprotection:
o Sphingolipids are especially important in the nervous system, where they form the myelin sheath
around nerve fibres, ensuring proper nerve conduction and protecting neurons.

Summary of Conjugated Lipids

Type of
Conjugated Structure Properties Functions Examples
Lipid
Amphipathic, form
Membrane structure, Phosphatidylcholine,
Glycerol backbone, two fatty lipid bilayers,
Phospholipids signaling, cell phosphatidylserine,
acids, phosphate group essential for
recognition sphingomyelin
membranes
Glycerol or sphingosine Amphipathic, Cell recognition,
Cerebrosides,
Glycolipids backbone, fatty acids, involved in cell blood type,
gangliosides
carbohydrate signaling neuroprotection
Lipids (phospholipids, Amphipathic, Lipid transport,
LDL, HDL, VLDL,
Lipoproteins cholesterol, triglycerides) + transport lipids in cholesterol
chylomicrons
proteins the bloodstream homeostasis
Amphipathic, Membrane structure,
Sphingosine backbone, fatty Sphingomyelin,
Sphingolipids involved in signaling,
acid, phosphate/carbohydrate cerebrosides, gangliosides
membrane structure neuroprotection

In summary, conjugated lipids, including phospholipids, glycolipids, lipoproteins, and sphingolipids, are integral to
a wide variety of biological functions, such as cell membrane structure, signaling, lipid transport, and cellular
communication. These lipids are essential for the proper functioning of cells and tissues in all living organisms.

GENERAL FUNCTIONS OF LIPIDS


CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

Structural:
i) They are components of the plasma/cell membrane.
ii) They form subcutaneous fat in the dermis of the skin hence insulating the body since they are poor
conductors of heat.
iii) They are components of the waxy cuticle in plants and insects there by preventing water loss (desiccation).
iv) They form a component of the myelin sheath of nerves hence playing a role in the transmission of impulses.
v) They protect delicate organs e.g. the heart and kidney from injury.
vi) They coat on fur of animals enabling it to repel water which would otherwise wet the organism.
vii) They are component of adipose tissue.
Physiological:
i) They provide energy through oxidation.
ii) They are solvents for fat soluble vitamins (ADEK).
iii) They are a good source of metabolic water to desert animals, young birds and reptiles while still in their shells.
iv) They are a constituent of the brown adipose tissue which provides heat for temperature regulation
(thermogenesis).
Other functions:
i) Some lipids provide a scent in plants which attracts insects for pollination.
ii) Wax is used by bees to construct honey combs.
iii) Wax from bees is used in the manufacture of candles.

QUESTION: WHAT PROPERTIES DO LIPIDS POSSES AS STORAGE COMPOUNDS?


i) They are compact taking up little space.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

ii) They are insoluble in water hence cannot be lost in solution.


iii) They are light to keep the weight to a minimum and allow buoyancy.
iv) They have a high calorific energy value.
v) They have a high hydrogen-oxygen content hence can yield a lot of water on oxidation.
PROTEINS
These are organic compounds of large molecular mass and insoluble in water. In addition to C, H and O, they
always contain N, usually S and sometimes P.
Whereas there are few carbohydrates and fats, the number of proteins is limitless e.g. a single bacterium may have
around 800 types of proteins while man has 10,000 types. This is because there are several amino acids which
may join in different patterns hence forming the various types of proteins.
Proteins are specific to each species hence determine the character of the species.
Proteins are not stored in the organism except in eggs and seeds where they are used to form new tissues. Proteins
form the structural basis of all living cells.
Their building blocks are the amino acids.
AMINO ACIDS
These are groups of many chemicals of which around 20 occur in proteins. They contain an amino group (NH2)
and a carboxyl group (COOH). Most amino acids have one of each and are therefore neutral but a few have more
amino groups than carboxyl making them alkaline or may have more carboxyl than amino groups making them
acidic.

Structure of amino acids

Where R is a variable
Amino acids are soluble in water and ionize to form ions.
The carboxyl end of the amino acid is acidic in nature. It will ionize in water to give H+. This will make
the COOH group negatively charged.
The amino end (NH2) is basic in nature. It attracts the H+ in solution making it positively charged. The ion
is now dipolar i.e. having a negative and a positive pole. Such ions are called zwitter ions i.e. the negative
and positive charges exactly balance and the amino acid ion has no overall charge i.e

. Zwitter ion (no overall charge)

Therefore in acidic solutions, an amino acid acts like a base and in alkaline solutions, it acts as an acid. In
neutral conditions found in the cytoplasm of most living organisms, the amino acid acts as both.
Amino acids therefore show both acidic and basic properties i.e. they are amphoteric. The overall charge of
the amino acid depends on the pH of the solution.
At some characteristic pH, the amino acid has no overall electric charge i.e. it exists as a zwitter ion. This
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

pH is called the isoelectric point of an amino acid.


If the pH falls below the iso-electric point i.e. the solution becomes more acidic, H+ are taken up by the
carboxyl ion. This reduces the concentration of the H+ in solution making the solution less acidic and the
amino acid gains an overall positive charge.
If the pH rises above the iso-electric point i.e. it becomes less acidic or more alkaline, hydrogen ions are
lost by the amino group. This increases the concentration of free H+ in the solution making it more acidic
and the amino acid gains an overall negative charge. Therefore being amphoteric, amino acids are buffers.
NOTE: a buffer solution is one which resists the tendency to alter its pH even when small amounts of acid
or base are added to it.
Questions: how do amino acids act as buffer solutions?
Amino acids make the proteins serve as buffers. The amphoteric nature of amino acids is useful biologically
as it means that they serve as buffers in solution resisting changes in PH. The buffer action depends on
concentration of hydrogen ions. When an acid is i.e more hydrogen ions(H+), the hydrogen ions(H+) are
accepted by the amino acids making them positively charged hence reducing the H+ concentration of the
solution. When a base is added, or a decrease in H+ concentration of the solution, the amino acid releases
H+ to the solution.
Types of amino acids
1. Essential Amino acids 2. Non-Essential amino acids
These are amino acids that cannot be synthesized by These are amino acids that are synthesized by the
the body and therefore got from the diet that the body through a process called transamination. They
organism feeds on. They include: include:
• Histidine • Tyrosine
• Isoleucine • Alanine
• Leucine • Glycine
• Serine
• Proline • Theonine
• Phenylalanine • Cystine
• Valine • Cystein
• Arginine • Aspartic acid
• lysine • Glutamic acid
• Methionine • Asparagine
• Tryptophan

Proteins can be classified into: first class proteins which contain all the essential amino acids e.g. from
beans and second-class proteins which are deficient of one or more essential amino acid.

Protein structures
There are 3 main protein structures i.e. primary structure, secondary structure and tertiary structure.
1. Primary structure:
It is a sequence of amino acids in a polypeptide chain. It is made up of 2 polypeptide chains held together
by di- sulphide bridges. The sequences of amino acids of a protein dictate its biological functions. Examples
of primary structures are insulin and lysosomes.
2. Secondary structure:
This involves folding or twisting of the polypeptide chains into a spiral shape or beta-pleated shape. It is
maintained by many ionic bonds which are formed between neighbouring COO- and NH3+ groups.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

(i) Spiral shape; proteins in this shape take the form of an alpha helix. They are hard but stretchable. The helical
structure is maintained by hydrogen bonds. Examples of such proteins include; keratin, collagen, etc.
keratin is found in hair, beaks, nails, feathers, claws, horns, etc.

(ii) Beta pleated sheets:


These result from the folding of two or more adjacently joined parallel polypeptide chains which are
stabilized by hydrogen bonds. They then get arranged into sheets. Proteins with this structure are very stable
and rigid (unstretchable) e.g fibroin protein found in silk. Beta pleated sheets have a flat zig zag structure.
They commonly occur in insoluble structural proteins but also in parts of some soluble proteins.

Tertiary structures
The polypeptide chain coils extensively forming a compact globular shape. This structure is maintained
by interaction of the four types of bonds i.e. ionic, hydrogen, di sulphide bonds and hydrophobic
interactions.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

The hydrophobic interactions are quantitatively the most important and occur when a protein folds to shield the
hydrophobic side groups from the aqueous surrounding and at the same time exposing hydrophobic side chains.
Quaternary structure
It is a combination of several polypeptide chains clumped together and associate with non-protein parts to
form complex proteins e.g. in haemoglobin.

Types of proteins
1. Fibrous proteins (plays structural roles)
These form long chains which may run parallel to one another being linked by cross bridges. They are very stable
molecules and have structural roles within the organism e.g. collagen in made of such proteins.
It has a primary structure which is a repeat of tri peptide sequence (glycine, proline and alanine) and forms a long
unbranched chain.
2. Globular proteins (plays metabolic roles)
They have a highly irregular sequence of amino acids in their polypeptide chains. Their shape is compact
and globular. All enzymes are globular proteins. Others include hormones and haemoglobin.
3. Conjugated proteins
These are proteins which incorporate other chemicals within their structure. The non-protein part is the
prosthetic group and plays a virtual role in the functioning of the proteins e.g.
Name of protein Where it is found Prosthetic group
Haemoglobin Blood Haem (iron)
Mucin Saliva Carbohydrate
Casein Milk Phosphoric acid
Cytochrome oxidase Electron carrier path way Copper
Nucleoplasm Ribosomes Nucleic acid
QUESTION: HOW DOES THE MOLECULAR STRUCTURE OF PROTEINS RELATE TO THEIR
ROLES?
i) Some proteins have a structural function, these are fibrous proteins with a secondary structure insoluble
in water and physically tough e.g. collagen in connective tissues, bone, tendons and cartilage. Other
structural proteins include keratin in feathers, nails, hair, horns, beaks and skin.
ii) Some proteins function as enzymes. These have a globular structure and are soluble in water e.g.
digestive enzymes like pepsin, respiratory and photosynthetic enzymes.
iii) Some proteins function as hormones regulating metabolic processes. These are globular and soluble in water
e.g. insulin which regulates metabolic activity.
iv) Some proteins functions as respiratory pigment. These are globular proteins with a quaternary structure
that increases their surface area for transport or storage of respiratory gases e.g. haemoglobin which
transports oxygen in blood and myoglobin that stores oxygen in muscles.
v) Some proteins are involved in transport and are globular with primary or tertiary structures e.g. serum
albumen that transports fatty acids and lipids in blood.
vi) Some proteins are involved in immunological responses hence protecting the body. These are globular
e.g. antibodies, fibrinogen and thrombin.
vii) Some proteins are contractile e.g. they are fibrous with a secondary structure e.g. myosin and actin
filaments in muscles.
viii) Storage proteins are toxins and soluble and water with a globular structure e.g. snake venom, bacteria
toxins, etc.
ix) Some proteins are insoluble in water e.g. ovalbumin that occurs in egg white, casein in milk, etc.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

x) Globular proteins form colloidal suspensions that hold molecules in position within cells e.g. proteins
in the cytoplasm of most cells where they are soluble in water and have a large surface area.
xi) Globular proteins in blood are buffers since they are soluble in water.
Differences between globular and fibrous proteins
Globular Fibrous
• Soluble in water • Insoluble in water
• Easily denatured by very high temperature • Not easily denatured by high temperature
• Functional in nature • Structural in nature
• Tertiary proteins • Secondary proteins
• Non identical polypeptide chain length • Identical polypeptide chain length
• Consist of compact and spherical molecules. • Consist of long fibrous molecules.
Denaturation of proteins
The dimensional structure of the protein is due to weak ionic and hydrogen bonds. Any agent which breaks
these bonds causes the three dimensional shape to be changed to a more fibrous form. This process is known
as denaturation.
In case the actual sequence of the amino acid is not altered but only the overall shape of the molecule is changed.
Factors causing protein denaturation
Factor Explanation Example
1. Heat Causes the atoms of the protein to vibrate Coagulation of albumen
more (egg white
thus breaking the hydrogen and ionic bond. becomes more fibrous).
2. pH When the pH is adjusted to the normal
isoelectric point for protein, its net charge will
be zero (zwitterion). If the pH is lowered far
below the isoelectric point, the protein will
lose its negative charge and contain only
positive charges. The like charges will repel
each other and prevent the protein from
aggregating as readily, preventing
formation of amine bonds.
3. Acids Addition of hydrogen ions in acids combine Souring of milk by acid and lowering
-
with COO of amino acids and form COOH pH of casein making it insoluble.
ionic bonds
are hence broken.
4. Alkalis Reduced number of H+ cause NH+ group to Souring of milk by
loose alkalis.
H+ to form NH2 therefore ionic bonds broken.
5. Inorganic Ions of heavy metals e.g. mercury and silver Enzymes are inhibited by being
chemicals combine with COO- groups destructing the destructed in presence of ions e.g.
ionic cytochrome
bonds. oxidase.
6. Organic Organic solvents alter hydrogen bonding with Alcohol denatures certain
chemicals a protein. bacterial
proteins. This is what makes it useful
for sterilization.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

7. Mechanical Physical movement can break hydrogen On stretching a hair, the hydrogen
force bonds. bonds in the keratin helix is extended
and hair
stretches.

FUNCTIONS OF PROTEINS
VITAL PROTEIN EXAMPLE FUNCTION
ACTIVITY
1. Nutrition • Digestive enzymes • catalyses, hydrolysis of proteins to peptides.
e.g. trypsin, amylase, • Helps to arrange chlorophyll molecules to
etc. receive unlimited light.
• Fibrous proteins in grana • Assists in transporting of food in filter feeder.
lamellae • Storage of proteins in milk.
• casein
2. Respiration and • Haemoglobin. • Transport of oxygen.
transport. • Myoglobin • Stores oxygen in muscles.
• Prothrombin/fibrinogen • Required for blood clotting.
• Antibodies. • Essential for defense.
3. Growth Hormones e.g. thyroxine Controls growth and metabolism.
4. Excretion Enzymes e.g. urease Catalyzes reaction in ornithine cycle and helps
in
protein break down and urea formation
5. Support and Actin/myosin Makes it easy for muscle contraction.
movement Collagen Gives strength with flexibility in tendons and
cartilage.
Keratin Tough for protection e.g. in scales, claws, nails,
hooves, etc.
Sceleratin Provide strength in insect exo-skeleton
6. Sensitivity and co- Hormones e.g. insulin Control of blood sugars
ordination. Vasopressin Control of blood pressure
Rhodopsin Visual pigments in retina.
8. Reproduction Hormones e.g. prolactin Induces milk production in mammals.
Chromatin Gives structural support to chromosomes.
Chitin Storage of proteins in seeds which nourishes
the
embryo.
Keratin Forms horns and anthers which are used for
sexual
display.

ENZYMES
Enzymes are biochemical catalysts made up of globular proteins. An enzyme is always associated with a
non-protein component known as co-factor which is tightly bonded to the enzyme.
Enzymes are organic compounds protein in nature that speed up the rate of biochemical reactions in the
body of an organism and remains unchanged at the end of the reaction.
Importance of enzymes
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

The rate at which some reactions occur in the body without enzymes is too slow to sustain life. Enzymes
therefore speed up the rate of the reaction without changing the product formed and the nature of
reaction i.e. an enzyme cannot make a reaction that would not occur to take place and it cannot make an
endothermic reaction exothermic but only ensures that products are formed in the shortest time possible.
They also control metabolic processes hence promoting normal body functions.

Mechanism of enzyme action


Each enzyme has a unique surface structure which provides a precise position known as active site, at which
the substrate can join the enzyme molecules to form an enzyme substrate complex.
This infinite contact is maintained until the reaction is complete. The precise and specific fit between
enzyme and substrate is sometimes compared with the lock and key mechanisms. There are two theories
put forward to describe the mechanism of enzyme action i.e.
(i) Lock and key hypothesis
(ii) Induced fit hypothesis
The lock and key mechanism
The widely accepted mechanism by which enzymes are known to work is the “key and lock” theory.
The theory suggests that the enzyme has a specific region known as the active site where the substrate fits
like a key fits in a lock. The substrate must have a complementary shape to the active site of the enzyme.
In this theory the key is analogous to the substrate and the lock to the enzyme. When the substrate combines
with the enzyme, an enzyme- substrate complex is formed. This breaks down to release the products and
the enzyme, which can pick other substrates.
Illustration

Advantages of the lock and key hypothesis


1. It explains why enzymes are specific in action i.e. only substrates with complementary shapes
to the active site fit into the active sites and are converted to products.
2. It explains why the rate of enzyme controlled reaction is affected by substrate concentration.
If all the active sites are in use, no more substrates a can fit or occupy the active site hence
the rate is constant.
3. It explains why and enzymes can be inhibited.
4. It explains why enzymes are able to lower the activation energy in a chemical reaction.

The induced fit theory


The bonds between the amino acids of the active site of the enzyme are relatively flexible. When
the substrate combines with an enzyme, the active site may mould into the shape of the substrate.
The theory says that when the substrate molecule enters the active site, it causes the enzyme to
change its shape so that the two molecules fit together more tightly. The induced fit hypothesis is
believed to make the substrate molecules more active because as the active site changes shape,
it presses on the substrate molecule exposing the weak bonds.
Enzyme inhibitors
Enzymes may be inactivated by substrates called inhibitors which interfere with catalytic
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

processes. This effect may be produced in several ways.


1. Active sites at the enzyme may be blocked by the formation of the enzyme inhibitor complex.
This is known as competitive inhibition and occurs when inhibitor molecule is structurally
similar to the usual substrate of the enzyme. The reaction can be reversed if the substrate
concentration is increased.
2. The inhibitor may react irreversibly with the enzyme to form an inactive non-enzymatic end
product. A small concentration of heavy metal ions combine permanently with the enzyme and
completely inhibit it.
3. The inhibitor may alter the shape of the enzyme at its point of activity so that the enzyme
substrate complexes cannot form. This is known as non-competitive enzyme inhibition.
These attach themselves not to the active site of the enzyme but elsewhere on the enzyme
molecule. These cause breakage of some bonds in the enzyme molecule leading to alteration
of the 3 dimensional structure and hence the shape of the enzyme molecule.
Change in the shape of the enzyme molecule leads to change of the shape of the active site.
Therefore the substrate can no longer fit in the active site.

An increase in the substrate concentration does not change the rate of reaction. This is because
the inhibitor alters/changes the shape of the enzyme and that of the active site permanently
whenever it comes into contact with the enzyme hence it leaves the active site non complementary.
Non competitive inhibitors are mostly non reversible inhibitors. Non competitive inhibitors include;
heavy metals (mercury, lead, silver, etc), cyanide, nerve gas, insecticides, herbicides, etc.

Importance of inhibitors
(i) They can be used in medicine and agriculture
(ii) They control metabolic pathways by regulating the different stages in them
(iii) They provide important information about the shapes and properties of enzymes.
2. End product inhibition
This takes place in some metabolic pathways when the end product combines with the first enzyme
controlling the first step of the pathway for its production so that further formation of the end
product is slowed or stopped. This is an example of negative feedback which is important in
regulation of body processes. The end product acts as an allosteric inhibitor.

These are enzymes that occur in two forms, i.e. active and inactive.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

The inactive form is shaped in such a way that the substrate will not fit into its active sites. Therefore
for such enzymes to work, it must be transformed into the active form.
Allosteric enzymes can be inhibited by molecules which do not combine with the active site but
with the other parts of the enzyme. In this case, the inhibitor prevents the enzymes from changing
into the active form, and substrates which bring about this are known as allosteric inhibitors.

Co-factors
Co-factors are non-protein components required by enzymes for their efficient functioning.
In some instances an enzyme must be associated with smaller molecule in order to function
properly. There are three types of co-factors:
i) Inorganic ions; e.g salivary amylase activity is increased by the presence of chloride ions.
ii) Prosthetic groups; these are non-protein organic molecules tightly bound to the active site e.g.
FAD, haem, etc.
Coenzymes; non-protein organic groups loosely associated with the enzyme, NAD and ATP. Prosthetic
groups and coenzymes act as carriers of groups of atoms.
Classification of enzymes
Each enzyme is given two names; a synthetic name based on the six classification groups. The
trivial names are derived by the following;

(i) Start with the name of the substrate on which the enzyme acts e.g. Succinate.
(ii) Add the name of the type of reaction which is catalysed e.g. dehydrogenation.
(iii) Convert the end of the last word to an …”ase” suffix e.g. Succinate Dehydrogenase.

Enzyme group Type of reaction Examples of enzymes


catalysed
1. Oxidoreductases Oxidation and reduction Dehydrogenase and oxidase
reaction
2. Transferases Transfer of chemical groups Transaminase and
phosphorylase
3. Hydrolases Hydrolysis reactions Maltase, amylases, lipase,
peptidase
4. Lyases Addition or removal of a decarboxylase
chemical
group by hydrolysis
5. Isomerases Arrangement of groups within Isomerases, mutases
the
molecule
6. Ligases Formation of bonds between synthetases
two molecules using energy
derived from
the breakdown of ATP

Enzymes are classified depending on the type of reaction they catalyze. The following are some of the
classes of enzymes.
1) Isomerase; these catalyze reactions involving isomerism
2) Phosphorylases; these catalyze reactions involving addition of a phosphate
3) Hydrogenases; these catalyze reactions involving addition of hydrogen.
4) Dehydrogenase; these catalyze reactions involving removal of hydrogen.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

5) Kinases; these catalyze reactions involving movement of molecules from one area to another.
6) Carboxylases; these catalyze reactions involving addition of Carbon dioxide.

Nomenclature of enzymes
Enzymes are named by adding a suffix “ase” to their substrates. A substrate is a substance, which
the enzyme acts upon, or simply it is the raw material for the enzyme.

Examples of enzymes and their substrates


Enzyme Substrate
Peptidase Peptides
Lipase Lipids
Maltase Maltose
Sucrase Sucrose
Lactase Lactose
Cellulase Cellulose
Some enzymes however retained their names they had before this convention. Such enzymes
include pepsin and trypsin.
Sometimes the enzymes digesting carbohydrates are generally called carbohydrases and those
digesting proteins as proteases.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

PROPERTIES OF ENZYMES
1) They are all protein in nature.
2) They are specific in their action i.e. they catalyze specific food i.e. Maltase on Maltose.
3) They speed up the rate of chemical reactions (they are catalysts).
4) They are effective even in small amounts.
5) They remain unchanged at the end of the reaction.
6) They are denatured by high temperatures since they are protein in nature
and are inactivated by low temperatures.
7) They are inactivated by inhibitor chemicals (poisons e.g. cyanide).
8) They work at a specific PH. (either acidic or alkaline).
9) Their reactions are reversible.
10) Their activity can be enhanced by enzyme activators e.g. chloride ions activate
amylase.

FACTORS AFFECTING THE RATE OF ENZYME CONTROLLED REACTIONS


1. Substrate concentration;
The rate of enzyme controlled reaction increases with increase in substrate concentration until
all the active sites of the enzyme are occupied by the substrate molecule. At this point the rate
of reaction can only be increased by increasing the enzyme concentration.

A: The rate of reaction increases with enzyme concentration because there are
free active sites into which more substrates fit increasing the rate of product
formation
B: The rate of reaction is constant because all the enzyme active sites are occupied
by substrates. Any more substrate molecules added will have no active sites to be
occupied hence constant rate of reaction. The limiting factor at this point is the low
enzyme concentration.
2. Temperature;
Within the physiological range (40c-400c) the rate of the enzyme controlled reaction
increases with increase in temperature. This is because temperature increases the
kinetic energy of reacting molecules leading to more collisions between the enzyme
and substrate molecules.
Beyond 400c, the rate of the reaction decreases with increase in temperature due
to Denaturation of the enzyme molecules.
Very high temperatures lead to breakage of some bonds that maintain the enzyme
structure. As a result, the 3 dimensional structure of the enzyme is altered leading
to a change in the shape of the active site.
The shape of the active site at this point can no longer fit in it hence no enzyme reaction.
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

3. Enzyme concentration;
Provided there is an excess of substrate molecules, the rate of an enzyme controlled
reaction increases with increase in enzyme concentration. This is because the
number of active sites increases which leads to increase in number of substrate
molecules that fit into and occupy the active sites hence increase in the rate of
product formation.
4. PH of the medium;
All enzymes work efficiently within a particular PH range. However there is an optimum PH
for each enzyme. Any deviation from the optimum PH results in Denaturation of the enzyme
hence decrease in the rate of reaction.

Enzyme Optimum PH
Pepsin 2.00
Sucrase 4.50
Enterokinase 5.59
Salivary amylase 4.80
Catalase 7.60
Chymotrypsin 7.00-
8.00
Pancreatic lipase 9.00

1. Enzyme inhibitors;
These lower the rate of enzyme controlled reactions or they may stop enzyme action
altogether.
2. Presence of cofactors;
For some enzymes, the rate of enzyme controlled reaction depends on cofactors.
How enzymes work
Enzymes work by lowering the activation energy to allow the reaction to take place.
Activation energy is the energy barrier that has to be overcome before a reaction
CHEMICALS OF LIFE NOTES S.5 2025 BY AKORA KENNETH

takes place. Since heat is usually the source of energy, enzymes make it possible
for reactions to take place at low temperature.
For enzymes to work, they lower the activation energy so that there is easy conversion of
reactants to products.

THE END

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