RUSANGU UNIVERSITY

SCHOOL OF SCIENCE AND TECHNOLOGY

CHEMISTRY DEPARTMENT

INTRODUCTION TO

BIOCHEMISTRY

MR MWEEMBA A.B
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 BACKGROUND

❖ Biochemistry is the branch of science that explores the chemical processes and substances that occur
within living organisms. It combines principles of chemistry and biology to understand the molecular
mechanisms by which cells and organisms’ function.
❖ This includes studying the structure and function of biomolecules like proteins, nucleic acids, lipids, and
carbohydrates, as well as their interactions and roles in processes such as metabolism, signal
transduction, and genetic expression. Biochemistry is fundamental to fields like medicine, genetics,
molecular biology, and biotechnology, as it helps to unravel the complexities of life at a molecular level.
❖ Biochemistry is, literally, the study of the chemistry of life. Although it overlaps other disciplines,
including cell biology, genetics, immunology, microbiology, pharmacology, and physiology, biochemistry
is largely concerned with a limited number of issues:

1. What are the chemical and three-dimensional structures of biological molecules?

2. How do biological molecules interact with each other?

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3. How does the cell synthesize and degrade biological molecules?
4. How is energy conserved and used by the cell?
5. What are the mechanisms for organizing biological molecules and coordinating their activities?
6. How is genetic information stored, transmitted, and expressed?
❖ Biochemistry, like other modern sciences, relies on sophisticated instruments to dissect the architecture
and operation of systems that are inaccessible to the human senses.

❖ In addition to the chemist’s tools for separating, quantifying, and otherwise analyzing biological
materials, biochemists take advantage of the uniquely biological aspects of their subject by examining
the evolutionary histories of organisms, metabolic systems, and individual molecules. In addition to its
obvious implications for human health, biochemistry reveals the workings of the natural world, allowing
us to understand and appreciate the unique and mysterious condition that we call life.

Studying biochemistry is important for students for various reasons, each contributing to a deeper
understanding of life processes and practical applications in numerous fields. Here are some reasons:

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1. Foundation of Life Sciences: Biochemistry provides the essential knowledge of the chemical processes
and substances that occur within living organisms, forming the basis for understanding biology,
medicine, and other life sciences.

2. Medical Applications: It is crucial for understanding the molecular basis of diseases, drug
development, diagnostics, and therapeutic interventions, making it indispensable for careers in
medicine, pharmacy, and healthcare.

3. Biotechnology and Innovation: Knowledge in biochemistry is key to advances in biotechnology,

including genetic engineering, agricultural improvements, and the development of new materials and
biofuels.

4. Understanding Metabolism: Biochemistry helps students understand how cells obtain energy, how
metabolic pathways are regulated, and how these processes are integrated within the body, which is
fundamental for health and disease management.

5. Research and Development: A solid grounding in biochemistry prepares students for research roles,
where they can contribute to discoveries in molecular biology, genetics, and other cutting-edge fields.

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6. Environmental Impact: Biochemistry aids in understanding the effects of chemicals on the
environment, helping develop sustainable practices and solutions to pollution, climate change, and
conservation efforts.

7. Nutritional Science: It is essential for understanding the biochemical basis of nutrition, how nutrients
are metabolized, and their impact on health, which is critical for dietetics and public health.

8. Pharmaceutical Industry: Biochemistry is fundamental in drug discovery, development, and testing,

providing the molecular understanding needed to create effective and safe medications.

9. Personal Health and Wellness: Students with knowledge in biochemistry can better understand their
health, make informed decisions about diet, exercise, and lifestyle, and comprehend the science
behind medical advice and treatments.

10. Interdisciplinary Connections: Biochemistry intersects with fields like physics, chemistry, and
engineering, fostering a versatile skill set that can be applied to diverse scientific and technological
challenges.

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 These reasons highlight the importance of biochemistry as a critical scientific discipline with wide-ranging
applications that impact various aspects of life and society.

❖ Any study of the chemistry of life must include a study of water. Biological molecules and the reactions
they undergo can be best understood in the context of their aqueous environment.

❖ Not only are organisms made mostly of water (about 70% of the mass of the human body is water), but
they are also surrounded by water on this “blue planet.”

PROPERTIES OF WATER

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 1. Water is polar:
Water molecules are polar, with partial positive charges on the hydrogens, a partial negative charge on the
oxygen, and a bent overall structure. This is because oxygen is more electronegative, meaning that it is
better than hydrogen at attracting electrons.
2. Water is an excellent solvent:

Water has the unique ability to dissolve many polar and ionic substances. This is important to all living things
because, as water travels through the water cycle, it takes many valuable nutrients along with it!

3. Water has high heat capacity:

It takes a lot of energy to raise the temperature of a certain amount of water by a degree, so water helps
with regulating temperature in the environment. For example, this property allows the temperature of
water in a pond to stay relatively constant from day to night, regardless of the changing atmospheric
temperature.

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4. Water has a high heat of vaporization:

Humans (and other animals that sweat) use water’s high heat of vaporization to cool off. Water is
converted from its liquid form to steam when the heat of vaporization is reached. Since sweat is made
mostly of water, the evaporating water absorbs excess body heat, which is released into the atmosphere.
This is known as evaporative cooling.

5. Water has cohesive and adhesive properties:

Water molecules have strong cohesive forces due to their ability to form hydrogen bonds with one another.
Cohesive forces are responsible for surface tension, the tendency of a liquid’s surface to resist rupture when
placed under tension or stress. Water also has adhesive properties that allow it to stick to substances other
than itself.

These cohesive and adhesive properties are essential for fluid transport in many forms of life. For example,
they allow nutrients to be transported to the top of a tree against the force of gravity.
6. Water is less dense as a solid than as a liquid:
As water freezes, the molecules form a crystalline structure that spaces the molecules further apart than in
liquid water. This means that ice is less dense than liquid water, which is why it floats.
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This property is important, as it keeps ponds, lakes, and oceans from freezing solid and allows life to
continue to thrive under the icy surface

7. Water has high tension:

This is due to the cohesion of water molecules. Due to this property, small organisms float or walk on the
water surface.

8. Water has a high heat of fusion: Water requires a loss of a lot of heat to freezing. This prevents freezing
and ice formation in the protoplasm even when exposed to very low temperatures.

8. Water is transparent:
This allows light to penetrate 200mt depth in sea and lakes. So plants carry on photosynthesis under
submerged conditions.

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9. Water is incompressible:
It helps organisms to tolerate pressure and compression. Because of this in earthworm water acts as hydro
skeleton. Loss or gain of water causes various plant movements like stomatal movement, seismonasty of
Mimosa leaves, etc.

Summary points
Studying water in biochemistry is crucial for several reasons, as water plays an integral role in the structure
and function of biological systems. Here are ten key points that highlight its importance:
1. Universal Solvent: Water's polarity makes it an excellent solvent, allowing it to dissolve and transport
various biomolecules, such as ions, proteins, and nucleic acids, which is essential for biochemical
reactions.
2. Hydrogen Bonding: Water's ability to form hydrogen bonds is fundamental to the stabilization of
protein structures, nucleic acid structures (like DNA and RNA), and enzyme-substrate interactions.
3. Thermoregulation: Water has a high specific heat capacity, which helps in maintaining stable internal
temperatures in organisms. This property is vital for homeostasis and the proper functioning of
enzymes, which have optimal temperature ranges.
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4. Role in Metabolic Reactions: Water is directly involved in many biochemical reactions, including
hydrolysis (breaking down molecules) and condensation (forming new bonds). For example, ATP
hydrolysis releases energy for cellular processes.
5. pH Balance and Buffering: Water contributes to the pH balance in biological systems. It dissociates

into H+ and OH- ions, which are involved in maintaining pH homeostasis, critical for enzyme activity

and metabolic processes.

6. Transport Medium: Water is the primary medium for transporting nutrients, waste products, and
gases (like oxygen and carbon dioxide) within cells and throughout the body via blood and lymphatic
fluids.
7. Structural Component: Water influences the three-dimensional structure of macromolecules. It helps
in maintaining the integrity of cell membranes and the proper folding of proteins, which is essential for
their function.
8. Cellular Environment: Water makes up a significant portion of the cytoplasm and extracellular fluids,
providing the medium in which biochemical reactions occur. It affects the behavior of ions, molecules,
and proteins within cells.

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9. Regulation of Biomolecular Interactions: The hydration shell around biomolecules like proteins and
nucleic acids influences how these molecules interact, affecting processes like enzyme activity,
signaling pathways, and molecular recognition.
10. Osmoregulation: Water is key in osmoregulation, the process by which cells and organisms
maintain fluid balance and proper cell turgor. This regulation is crucial for cellular stability and
function, especially in varying environmental conditions.

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AMINO ACIDS CLASSIFICATION
AND PROPERTIES

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 WHAT ARE AMINO ACIDS.
❖ Amino acids are organic molecules that serve as the building blocks of proteins, which are essential
for numerous biological processes. Each amino acid has a basic structure composed of:

❖ A central carbon atom (C) known as the alpha carbon.

❖ An amino group (-NH₂) attached to the central carbon.
❖ A carboxyl group (-COOH) attached to the central carbon.
❖ A hydrogen atom (H) attached to the central carbon.
❖ A side chain (R group) attached to the central carbon, which varies among different amino acids and
determines their unique properties.

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❖ There are 20 standard amino acids that are used to synthesize proteins in organisms. These amino
acids can be categorized based on the properties of their side chains, such as nonpolar, polar, acidic,
or basic.

❖ Amino acids are linked together by peptide bonds during protein synthesis, forming long chains
called polypeptides. These polypeptide chains fold into specific three-dimensional structures to
become functional proteins. The sequence and composition of amino acids in a protein determine
its structure and function.

❖ In addition to their role in protein synthesis, amino acids are also involved in various metabolic
pathways, acting as precursors for the synthesis of other biomolecules, neurotransmitters, and
hormones.

❖ Amino acids are organic compounds containing

amine [- NH 2 ]

carboxyl [-COOH]

side-chain [R group]
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❖ The major key elements in amino acids are carbon,
hydrogen, nitrogen, oxygen.

BASIC STRUCTURE[SKELETON]

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 Classification of Amino Acids
Classification of amino acids gives the grouping between 20 acids and a basic
outline for grouping.

❖ It makes a clear idea to pick the amino acid type

❖ This is much useful for biochemists for the easy understanding between each amino
acid.

❖ About 500 amino acids are known (though only 20 appear in the genetic code) and
can be classified in many ways.

❖ Amino acids are the building blocks of proteins and play essential roles in various biological
processes. They can be classified in several ways based on their properties, structure, and
chemical characteristics. Here is a detailed breakdown:

Based on the nature of the R group, amino acids are classified into various categories:
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 ✓ Classification Based on Polarity and Charge
Nonpolar (Hydrophobic) Amino Acids

• Characteristics: These amino acids have side chains that do not interact well with water,
making them hydrophobic. They are usually found in the interior of proteins, away from the
aqueous environment.

• Examples:

o Glycine (Gly, G)

o Alanine (Ala, A)

o Valine (Val, V)

o Leucine (Leu, L)

o Isoleucine (Ile, I)

o Methionine (Met, M)

o Phenylalanine (Phe, F)

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 o Tryptophan (Trp, W)

o Proline (Pro, P)

Polar (Hydrophilic) Uncharged Amino Acids

• Characteristics: These amino acids have side chains that can form hydrogen bonds with water,
making them hydrophilic but uncharged at physiological pH.

• Examples:

o Serine (Ser, S)

o Threonine (Thr, T)

o Cysteine (Cys, C)

o Asparagine (Asn, N)

o Glutamine (Gln, Q)

o Tyrosine (Tyr, Y)

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Polar (Hydrophilic) Charged Amino Acids

• Positively Charged (Basic) Amino Acids:

o Characteristics: These amino acids have side chains that carry a positive charge at
physiological pH (The PH that normally prevails in the human body; it is approximately
7.4).

o Examples:

▪ Lysine (Lys, K)

▪ Arginine (Arg, R)

▪ Histidine (His, H)

• Negatively Charged (Acidic) Amino Acids:

o Characteristics: These amino acids have side chains that carry a negative charge at
physiological pH.

o Examples:

▪ Aspartic acid (Asp, D)

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 ▪ Glutamic acid (Glu, E)

✓ Classification Based on Nutritional Requirements

Essential Amino Acids

These amino acids cannot be synthesized by the human body and must be obtained from the diet.
There are 9 essential amino acids:

• Histidine (His, H)

• Isoleucine (Ile, I)

• Leucine (Leu, L)

• Lysine (Lys, K)

• Methionine (Met, M)

• Phenylalanine (Phe, F)

• Threonine (Thr, T)

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 • Tryptophan (Trp, W)

• Valine (Val, V)

Non-Essential Amino Acids

These amino acids can be synthesized by the body. Examples include:

• Alanine (Ala, A)

• Asparagine (Asn, N)

• Aspartic acid (Asp, D)

• Glutamic acid (Glu, E)

Conditionally Essential Amino Acids

These amino acids are usually synthesized by the body but may become essential under specific
conditions such as illness or stress. Examples include:

• Arginine (Arg, R)

• Cysteine (Cys, C)

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 • Glutamine (Gln, Q)

• Glycine (Gly, G)

• Proline (Pro, P)

• Tyrosine (Tyr, Y)

✓ Classification Based on Metabolic Fate

Glucogenic Amino Acids

• Characteristics: These amino acids can be converted into glucose through gluconeogenesis.

• Examples: Alanine, Serine, Cysteine, Histidine, and others.

Ketogenic Amino Acids

• Characteristics: These amino acids can be converted into ketone bodies.

• Examples: Leucine and Lysine.

Both Glucogenic and Ketogenic Amino Acids

• Characteristics: These amino acids can produce both glucose and ketone bodies.

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 • Examples: Isoleucine, Phenylalanine, Tyrosine, and Tryptophan.

✓ Classification Based on Side Chain Chemistry

Aliphatic Amino Acids

• Characteristics: The side chain is composed of linear or branched carbon atoms.

• Examples: Glycine, Alanine, Valine, Leucine, Isoleucine.

Aromatic Amino Acids

• Characteristics: The side chain contains a benzene ring or similar structure.

• Examples: Phenylalanine, Tyrosine, Tryptophan.

Sulfur-Containing Amino Acids

• Characteristics: These amino acids contain sulfur in their side chains.

• Examples: Cysteine, Methionine.

Hydroxyl-Containing Amino Acids

• Characteristics: These amino acids contain a hydroxyl (-OH) group in their side chains.

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 • Examples: Serine, Threonine, Tyrosine.

✓ Special Amino Acids

• Glycine (Gly, G): The simplest amino acid with a hydrogen atom as its side chain. It is not chiral
and adds flexibility to protein structures.

• Proline (Pro, P): A unique amino acid with a cyclic structure that forms a bond between the α-
carbon and the nitrogen of the amino group, restricting its flexibility and often introducing
kinks into protein structures.

• Cysteine (Cys, C): Contains a thiol (-SH) group, which can form disulfide bonds (S-S) that are
important for protein stability.

These classifications provide an overview of how amino acids differ in their properties and behavior
in biological systems, which is essential for understanding protein structure, function, and
metabolism in biochemistry.

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 PROTEINS
❖ Proteins are the most abundant organic molecules in animals, playing important roles in all aspects
of cell structure and function. Proteins are biopolymers of a-amino acids, so named because the
amino group is bonded to the ἁ carbon atom, next to the carbonyl group. The physical and
chemical properties of a protein are determined by its constituent amino acids.

❖ Proteins are large, complex molecules made up of amino acids and are essential to the structure,
function, and regulation of the body's cells, tissues, and organs.

❖ The individual amino acid subunits are joined by amide linkages called peptide bonds. Below is the
general structure of an ἁ-amino acid and a protein.

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Formation of proteins

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➢ Twenty percent of the human body is made up of proteins. Proteins are the large, complex molecules
that are critical for normal functioning of cells.

➢ They are essential for the structure, function, and regulation of the body’s tissues and organs.

➢ Proteins are made up of smaller units called amino acids, which are building blocks of proteins. They are
attached to one another by peptide bonds forming a long chain of proteins.

➢ As its name implies, an amino acid is an organic compound containing an amino group and a carboxyl
group.

➢ A protein is typically composed of at least 50 amino acids linked together in a chain, though smaller
chains of amino acids, called peptides, can range from just two to about 50 amino acids. Larger chains,
containing hundreds or even thousands of amino acids, form more complex proteins. In general, the
term "protein" is usually reserved for polypeptides that consist of 50 or more amino acids.

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Here are examples of different types of proteins based on their functions:

1. Enzymes

• Amylase: Helps break down carbohydrates (found in saliva).

• DNA polymerase: Involved in DNA replication.

2. Structural Proteins

• Collagen: Provides structural support in connective tissues (like skin and bones).

• Keratin: Found in hair, nails, and the outer layer of skin.

3. Transport Proteins

• Hemoglobin: Transports oxygen in the blood.

• Albumin: Helps maintain blood osmotic pressure and transports substances in the bloodstream.

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4. Signaling Proteins

• Insulin: Regulates blood sugar levels.

• Epidermal Growth Factor (EGF): Stimulates cell growth and division.

5. Motor Proteins

• Myosin: Facilitates muscle contraction.

• Kinesin: Transports cellular cargo along microtubules.

6. Defense Proteins

• Antibodies (Immunoglobulins): Protect the body by recognizing and neutralizing pathogens.

• Lysozyme: Breaks down bacterial cell walls.

7. Storage Proteins

• Ferritin: Stores iron in the liver.

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• Casein: A storage protein found in milk.

Each protein type plays a critical role in various biological processes.

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 FUNCTIONS OF PROTEINS
❖ Proteins are by far the most important of all biological compounds. The very word “protein” is derived
from the Greek proteios, meaning “of first importance,”.

❖ Proteins play a multitude of vital roles in biological systems, owing to their diverse structures and
functions. Below are some of the key functions of proteins with brief discussions:

Enzymatic Activity
• Function: Proteins act as enzymes, catalyzing biochemical reactions by lowering activation energy.
• Example: Amylase, found in saliva, breaks down starches into sugars.
• Importance: Enzymes are critical for metabolism, facilitating thousands of reactions that would
otherwise occur too slowly to sustain life.
Structural Support
• Function: Proteins provide structure and support to cells and tissues.
• Example: Collagen, a major component of connective tissues, gives skin and bones their tensile

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 strength.
• Importance: Structural proteins maintain the integrity of cells, tissues, and organs.
Transport and Storage
• Function: Proteins transport molecules across cellular membranes or within the body.
• Example: Hemoglobin transports oxygen in the blood.
• Importance: Transport proteins are crucial for maintaining homeostasis, ensuring that essential
molecules like gases, ions, and nutrients reach their destination.
Regulation of Gene Expression
• Function: Some proteins regulate the transcription and translation of genes.
• Example: Transcription factors bind to DNA and control the expression of specific genes.
• Importance: Gene regulatory proteins ensure that the correct proteins are made at the right time and
in the right amounts.
Hormonal Function
• Function: Proteins can act as hormones, which are signaling molecules that regulate physiological

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 processes.
• Example: Insulin, a protein hormone, regulates blood glucose levels.
• Importance: Hormonal proteins coordinate the body's responses to stimuli and maintain homeostasis.
• Erythropoietin (EPO) is a glycoprotein hormone, naturally produced by the peritubular cells of the kidney, that
stimulates red blood cell production.
Immune Response
• Function: Proteins are involved in recognizing and neutralizing foreign substances like bacteria and
viruses.
• Example: Antibodies (immunoglobulins) bind to pathogens, marking them for destruction by the
immune system.
• Importance: The immune system relies heavily on proteins to protect the body from infections.
Movement
• Function: Proteins enable cellular and organismal movement.
• Example: Actin and myosin are responsible for muscle contraction.
• Importance: Proteins facilitate essential movements, from the contraction of muscles to the
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 intracellular transport of vesicles.
Cell Signaling
• Function: Proteins mediate communication between cells through signal transduction pathways.
• Example: Receptor proteins like G-protein coupled receptors (GPCRs) respond to external signals and
activate intracellular responses.
• Importance: Signal transduction proteins enable cells to respond to environmental changes, and
coordinate growth, and development.
Buffering
• Function: Proteins help maintain the acid-base balance in the body.
• Example: Hemoglobin acts as a buffer, helping to regulate blood pH by binding or releasing hydrogen
ions.
• Importance: Buffering proteins are vital in keeping physiological systems within the necessary pH
range.

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Cell Adhesion
• Function: Proteins facilitate the adhesion of cells to each other and the extracellular matrix.
• Example: Cadherins mediate cell-cell adhesion in tissues.
• Importance: Cell adhesion proteins are essential for tissue formation, wound healing, and immune
responses.

Receptor Function
• Function: Proteins function as receptors that detect and respond to chemical signals from the
environment or other cells.
• Example: Insulin receptors on cell membranes bind insulin, initiating a signaling cascade that regulates
glucose uptake.
• Importance: Receptor proteins are key components of cellular communication, allowing cells to
respond to hormones, neurotransmitters, and other external signals.

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Storage of Ions and Molecules
• Function: Some proteins store important ions and molecules for future use.
• Example: Ferritin stores iron in the liver and releases it when needed.
• Importance: Storage proteins ensure that vital resources like minerals and nutrients are available
when the body needs them, preventing deficiencies.
Energy Source
• Function: In times of starvation or caloric deficiency, proteins can be broken down and used as an
energy source.
• Example: In muscle tissue, proteins can be broken down into amino acids and used for
gluconeogenesis, the production of glucose from non-carbohydrate sources.
• Importance: While proteins are not the primary source of energy (usually carbohydrates and fats serve
this role), they can be catabolized to provide energy when necessary.

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Defense and Protective Function
• Function: Proteins serve protective roles by forming physical barriers or binding to foreign substances.
• Example: Keratin, found in the skin, hair, and nails, provides a protective barrier against environmental
damage.
• Importance: Protective proteins safeguard the body from injury, pathogens, and other external
threats.
Chaperone Function
• Function: Some proteins assist other proteins in folding correctly and maintaining their proper shape.
• Example: Heat shock proteins (HSPs) help other proteins fold properly under stress conditions, such as
high temperatures.
• Importance: Chaperone proteins prevent misfolding and aggregation, which could lead to diseases like
Alzheimer's or cystic fibrosis, where protein misfolding plays a major role.

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Membrane Transport
• Function: Proteins regulate the movement of substances across cell membranes.
• Example: Ion channels, such as sodium and potassium channels, allow the controlled flow of ions in
and out of cells, maintaining electrical balance.
• Importance: Membrane transport proteins are critical for nutrient uptake, waste removal, and
maintaining the cell's electrochemical gradient, necessary for functions like nerve transmission.
Cell Cycle Regulation
• Function: Proteins control the progression of the cell cycle, ensuring cells divide correctly.
• Example: Cyclins and cyclin-dependent kinases (CDKs) regulate cell cycle transitions.
• Importance: Proper cell cycle regulation is essential for growth, repair, and reproduction, and defects
in these proteins can lead to conditions like cancer.
Protein Turnover and Degradation
• Function: Proteins like ubiquitin tag damaged or unneeded proteins for degradation, ensuring cellular
proteins are properly maintained.

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 • Example: The ubiquitin-proteasome system targets and breaks down damaged proteins.
• Importance: Protein degradation is essential for clearing faulty proteins, preventing their
accumulation, and regulating protein levels within the cell.

Osmotic Balance
• Function: Proteins help regulate water and ion balance within cells and tissues.
• Example: Albumin, a protein in blood plasma, helps maintain osmotic pressure, ensuring proper fluid
distribution between blood and tissues.
• Importance: Maintaining osmotic balance is critical for preventing conditions like edema (fluid
retention) and ensuring the stability of blood pressure.
Detoxification
• Function: Certain proteins detoxify harmful substances within the body.
• Example: Cytochrome P450 enzymes in the liver metabolize drugs and toxins, making them easier for
the body to excrete.

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 • Importance: Detoxification proteins protect the body from harmful chemicals and drugs, ensuring that
toxic compounds are neutralized and eliminated.
Proteins are thus indispensable for nearly all biological processes, serving as catalysts, structural elements,
signaling molecules, and more. Their versatility stems from the variety of structures they can adopt, which
allows them to fulfill a wide range of functions.

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 The two major classes of proteins are:
1. Fibrous Proteins: These proteins are typically elongated and insoluble in water. They serve structural
roles in cells and tissues. Examples include collagen (found in connective tissues), keratin (in hair,
nails, and skin), and elastin (in ligaments and skin).
2. Globular Proteins: These proteins are more compact, soluble in water, and generally have functional
roles in biochemical processes. Examples include enzymes (such as amylase and DNA polymerase),
antibodies, and hemoglobin (which transports oxygen in the blood).
Fibrous proteins focus on structural support, while globular proteins are involved in dynamic biological
functions.

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 Structure of proteins
❖ To understand how a protein gets its final shape or conformation, we need to understand the four levels of protein
structure: primary, secondary, tertiary, and quaternary.

❖ The structure of proteins can be categorized into four levels:

1. Primary Structure:
• Description: This is the linear sequence of amino acids in the polypeptide chain, linked by peptide
bonds.
• Key Feature: The specific order of amino acids is determined by the genetic code and is unique for
each protein.
2. Secondary Structure:
• Description: This refers to the local folding or coiling of the polypeptide chain into specific structures.
• Types:
o Alpha-helix (α-helix): A right-handed coil where the backbone is wound around an imaginary
axis.
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 o Beta-sheet (β-sheet): Strands of the polypeptide chain align side by side, forming sheet-like
structures.
• Key Feature: Stabilized by hydrogen bonds between the carbonyl oxygen and amide hydrogen in the
backbone.
3. Tertiary Structure:
• Description: This is the overall 3D structure of a single polypeptide chain. It is formed by the folding
and interactions between side chains (R groups) of amino acids.
• Key Interactions:
o Hydrophobic interactions
o Hydrogen bonds
o Ionic bonds
o Disulfide bridges (covalent bonds between cysteine residues)
• Key Feature: Determines the protein's specific shape and function.

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4. Quaternary Structure:
• Description: This structure involves the arrangement and interaction of multiple polypeptide chains
(subunits) to form a functional protein complex.
• Key Feature: Proteins with more than one polypeptide chain exhibit this structure. Examples include
hemoglobin and DNA polymerase.
Example: Hemoglobin
• Hemoglobin's quaternary structure consists of four subunits, each with its own tertiary structure,
working together to transport oxygen in the blood.
The specific structure of a protein determines its function. Misfolding or incorrect formation of these
structures can lead to diseases such as Alzheimer's or prion diseases.

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Several side effects could arise due to the imbalance in nutrient intake and the strain it places on certain
bodily systems. Here are some potential side effects of excessive intake of proteins (commonly through diet
or supplementation):
1. Kidney Strain
• Dehydration: High protein intake can increase the body's need for water, which may lead to
dehydration if not adequately addressed.
• Kidney Damage: For people with preexisting kidney conditions, excess protein can exacerbate kidney
strain, potentially worsening renal function due to increased filtration load.
2. Digestive Issues
• Constipation: High-protein diets, particularly those low in fiber (like diets heavy in animal protein),
may lead to constipation.
• Indigestion and Bloating: Consuming large quantities of protein, especially from certain sources like
protein powders or shakes, may cause digestive discomfort, gas, or bloating.

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3. Nutrient Imbalance
• Reduced Carbohydrate and Fat Intake: Focusing too much on protein could lead to a deficiency in
other essential macronutrients like carbohydrates and fats, which are crucial for energy and other
metabolic functions.
• Micronutrient Deficiency: A diet that prioritizes protein over a balanced variety of foods could lead to
insufficient intake of essential vitamins and minerals (e.g., fiber, antioxidants).
4. Bone Health
• Calcium Loss: Excessive protein intake, especially from animal sources, might lead to calcium leaching
from bones due to the body's need to balance the acid load caused by certain amino acids.
5. Weight Gain
• Excess Calories: Although protein is essential for muscle maintenance and other bodily functions,
consuming more protein than the body needs may result in excess calorie intake, leading to weight
gain if energy expenditure doesn't match.

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6. Heart Health
• High Saturated Fat Intake: Diets rich in animal-based proteins, like red meat or processed meats, often
come with high levels of saturated fats, which can increase cholesterol levels and lead to
cardiovascular diseases.
7. Liver Strain
• Ammonia Build-Up: The liver metabolizes protein, and excessive protein consumption can lead to an
accumulation of ammonia, which, if not processed efficiently, may be toxic, particularly for individuals
with liver dysfunction.
8. Impact on Metabolism
• Ketosis: High-protein, low-carbohydrate diets may induce ketosis, a metabolic state where the body
relies on fat for energy. While this can be beneficial for some, it may cause side effects such as
headaches, fatigue, and bad breath.

THE END

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