PROTEIN: THE
BUILDING BLOCKS
OF LIFE
Subject: Nutrition & Dietetics
Topic: Comprehensive Analysis of Proteins
Prepared for Nutrition & Dietetics Examination
Research & Study Assignment
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Table of Contents
1. Introduction 3
2. Definition of Protein 4
3. Classification of Protein 5
4. Functions of Protein 7
5. Sources of Protein 9
6. Daily Requirement of Protein 10
7. Protein Deficiency Disorders 11
8. Digestion and Absorption 12
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1. Introduction
Proteins are the most abundant organic molecules of the living system. They occur
in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life. Derived from
the Greek word 'Proteios', meaning 'holding first place' or 'primary', proteins are
indeed the primary molecules of life. In the study of Nutrition and Dietetics, protein
occupies a central role because it is involved in virtually every physiological
process. Unlike carbohydrates and fats, which primarily serve as fuel, proteins are
the structural components of tissues. Every cell in the human body contains
protein. It is a major component of the skin, muscles, organs, and glands. Protein
is also found in all body fluids, except bile and urine. We need protein in our diet to
help our body repair cells and make new ones. Protein is also important for growth
and development in children, teens, and pregnant women.
In the dietary context, proteins are categorized as macronutrients, alongside
carbohydrates and lipids. However, their role is distinct. While carbohydrates and
lipids are efficiently stored as energy reserves (glycogen and adipose tissue), the
body maintains no specialized storage for proteins. Instead, proteins are functional
components. Every gram of protein in the body serves a specific purpose, whether
as a structural fiber or a catalytic enzyme. Therefore, a regular supply of protein
through the diet is essential for the continuous turnover and maintenance of these
physiological structures.
Historically, the nitrogenous nature of proteins was first recognized in the
early 19th century. Antoine Fourcroy and others identified a distinct class of
biological molecules that coagulated upon heating, which we now know as
proteins.
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2. Definition
Proteins are high molecular weight, complex nitrogenous organic compounds.
Chemically, they are polymers of alpha-amino acids linked together by peptide
bonds. While carbohydrates and lipids are composed of Carbon, Hydrogen, and
Oxygen, proteins characteristically contain Nitrogen (averaging about 16%),
alongside Carbon, Hydrogen, Oxygen, and often Sulfur and Phosphorus. The basic
unit of protein is the amino acid. There are about 20 standard amino acids that
combine in various sequences to form thousands of different proteins. These are
often categorized into 'Essential Amino Acids' (which the body cannot synthesize
and must be obtained from diet) and 'Non-Essential Amino Acids' (which the body
can synthesize).
The Amino Acid Structure
An amino acid consists of a central carbon atom (the alpha-carbon), a hydrogen
atom, an amino group (-NH2), a carboxyl group (-COOH), and a variable side chain
known as the R-group. The nature of this R-group determines the unique properties
of each amino acid.
When these amino acids link together, the carboxyl group of one molecule reacts
with the amino group of another, releasing a molecule of water and forming a
Peptide Bond. A long chain of these amino acids is termed a Polypeptide.
Essential Amino Acids include: Phenylalanine, Valine, Threonine, Tryptophan,
Isoleucine, Methionine, Histidine, Arginine, Leucine, and Lysine (The
mnemonic 'PVT TIM HALL' is often used).
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3. Classification of Protein
I. Based on Chemical Composition
Type Description Examples
Simple On hydrolysis, they yield only amino acids.
Simple
Proteins Examples: Albumins, Globulins.
Contain a non-protein group (prosthetic group)
Conjugated
attached to the protein. Examples: Conjugated
Proteins
Nucleoproteins, Glycoproteins, Lipoproteins.
Produced by the partial hydrolysis or
Derived
denaturation of native proteins. Examples: Derived
Proteins
Peptones, Proteoses.
II. Based on Nutritional Value
Dietary proteins are not created equal. Their value is determined by the presence
and ratio of the ten essential amino acids.
• Complete Proteins (High Biological Value - HBV): Contain all essential
amino acids in sufficient amounts. Primarily found in animal sources like
eggs, milk, and meat.
• Partially Incomplete Proteins: Lack one or more essential amino acids. Many
plant proteins fall into this category.
• Incomplete Proteins: Totally lack one or more essential amino acids and
cannot support growth or even maintain life if consumed alone.
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III. Based on Shape and Solubility
1. Fibrous Proteins: These are long, thread-like molecules that are tough and
insoluble in water. They serve structural and protective roles. Examples include
Collagen in connective tissue and Keratin in hair and nails.
2. Globular Proteins: These are spherical or oval-shaped and are generally soluble
in water or dilute salt solutions. They usually have dynamic roles such as transport,
catalysis, and regulation. Examples include Enzymes and Myoglobin.
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4. Functions of Protein
The biological importance of proteins cannot be overstated. They are involved in
nearly every aspect of life. Below are the primary physiological functions:
Growth and Maintenance
Proteins are necessary for the creation and repair of new tissues. During periods of
growth (infancy, childhood, pregnancy), protein needs are highest. Even in adults,
proteins are constantly replaced to maintain cellular integrity.
Enzymatic Action
Most enzymes are proteins. They catalyze biochemical reactions necessary for
metabolism, digestion, and energy production.
Hormonal Regulation
Several hormones are protein-based (e.g., Insulin, Glucagon, Growth Hormone).
They act as chemical messengers, coordinating activities between different parts
of the body.
Structural Role
Proteins like Collagen, Keratin, and Elastin provide structure and strength to skin,
hair, nails, bones, and connective tissues.
Transport and Storage
Hemoglobin (protein) transports oxygen in the blood. Ferritin stores iron.
Lipoproteins transport lipids across the bloodstream.
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Immune Function
Antibodies (Immunoglobulins) are proteins that help the body fight infections and
foreign invaders.
Fluid and Acid-Base Balance
Albumin and globulin in the blood pull water into tissues and maintain osmotic
pressure. Proteins also act as buffers to prevent radical changes in blood pH.
Energy Production: Although not the primary role, protein can be broken
down to provide energy (4 kcal per gram) when carbohydrate and fat stores
are insufficient.
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5. Sources of Protein
To maintain health, humans must consume protein from various food sources.
These sources are divided into animal-based and plant-based origins.
Animal Sources (High Quality)
• Eggs (Standard Protein)
• Milk and Dairy products (Paneer, Cheese, Curd)
• Lean Meats (Chicken, Turkey)
• Fish
• Organ meats
Plant Sources
• Pulses and Legumes (Soybeans, Chickpeas, Lentils)
• Nuts and Seeds (Almonds, Walnuts, Chia seeds)
• Cereals (Quinoa, Wheat, Rice - contain smaller amounts)
• Spirulina (Algal source)
Mutual Supplementation: For vegetarians, combining two or more incomplete
protein sources (e.g., rice and dal) can provide a complete profile of essential
amino acids.
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6. Daily Requirement of Protein
The Recommended Dietary Allowance (RDA) varies based on age, sex,
physiological state, and body weight.
Group Age/State Requirement (g/kg/day)
Group Age/State Requirement (g/kg/day)
Infants 0-6 months 1.16
Children 1-3 years 0.97
Adolescents 13-15 years 0.85
Adults Sedentary/Moderate 0.83 - 1.0
Pregnant Women 2nd & 3rd Trimester Add +25g to normal RDA
Lactating Mothers 0-6 months Add +19g to normal RDA
Factors influencing protein requirements include age, physical activity level, muscle
mass, illness, and injury. Professional athletes and those recovering from surgery
may requires significantly higher intake.
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7. Protein Deficiency Disorders
PEM is a range of pathological conditions arising from coincident lack of varying
proportions of protein and calories, occurring most frequently in infants and young
children.
1. Kwashiorkor
Derived from a Ga word meaning 'the sickness the baby gets when the new baby
comes', referring to weaning.
• Edema (swelling, especially in legs and face)
• Protruding belly (pot belly)
• Skin changes (flaky-paint dermatitis)
• Hair changes (loss of pigmentation, 'flag sign')
• Enlarged fatty liver
• Irritability and lethargy
2. Marasmus
Severe deficiency of both energy and protein.
• Extreme muscle wasting
• Loss of subcutaneous fat (skin and bones appearance)
• Old man's face (wrinkled skin)
• Severe growth retardation
• Alert but hungry appearance
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Prevention and Treatment: These conditions can be managed through
balanced diet enrichment with protein-rich supplements, gradual refeeding,
and education on weaning practices.
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8. Digestion and Absorption
The human body cannot absorb whole protein molecules. They must be broken
down into their constituent amino acids through a systematic process of digestion.
Digestion Process
Mouth: No chemical digestion of protein occurs in the mouth. Mechanical chewing
breaks down larger pieces of food.
Stomach: Contact with Hydrochloric acid (HCl) denatures proteins. Pepsinogen is
converted to Pepsin, which breaks proteins into smaller polypeptides.
Small Intestine: The bulk of digestion occurs in the small intestine. Pancreatic
enzymes (Trypsin, Chymotrypsin, Carboxypeptidase) and brush border enzymes
(Aminopeptidases, Dipeptidases) further break polypeptides into dipeptides,
tripeptides, and free amino acids.
Absorption
Amino acids are absorbed through the intestinal wall (primarily jejunum) via active
transport into the portal bloodstream and transported to the liver.
Once in the liver, amino acids are either used to synthesize new body proteins,
converted to other molecules like glucose, or used for energy production after the
removal of the nitrogen group (deamination).
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