A

Project on

STUDY OF PROTEIN AS BULIDING BLOCK

For

The Submission of the Practical Fulfillment of the

AISSCE CBSE Practical Examination

In

CHEMISTRY

Submitted By

AISHWARYA NISHAD

Under the supervision

Of

DR. ANIRUDH PORVAL

P.G.T CHEMISTRY

Gayatri Vidyapeeth

GAYATRI VIDYAPEETH, SHANTIKUNJ

HARIDWAR-249411

2022-23
 CERTIFICATE
THIS is to certify that, AISHWARYA NISHAD the student of class “XII
SCIENCE”, during the year 2022-23, has successfully completed her
investigatory project on STUDY OF PROTEIN AS A BUILDING BLOCK,
for the fulfillment of board examination conducted by C.B.S.E. During the
tenure, original and genuine investigation work has been carried out to investigate
about the subject matter and investigation has been completed solely, sincerely
and satisfactorily.

DR. ANIRUDH PORVAL

P.G.T CHEMISTRY
GAYATRIVIDYAPEETH,
SHANTIKUNJ, HARIDWAR

CERTIFICATE
THIS is to certify that, AISHWARYA NISHAD the student of class “XII
SCIENCE”, during the year 2022-23, has successfully completed her
investigatory project on STUDY OF PROTEIN AS A BUILDING BLOCK,
for the fulfillment of board examination conducted by C.B.S.E. During the
tenure, original and genuine investigation work has been carried out to investigate
about the subject matter and investigation has been completed solely, sincerely
and satisfactorily.

MR. S. R. SINHA

PRINCIPAL

GAYATRI VIDYAPEETH,

SHANTIKUNJ, HARIDWAR
 ACKNOWLEDGEMENT
Presentation, inspiration and motivation have always played a Key role in the
Success of my venture. In the success sand final Outcome of this project required
lots of guidance and assistance from people and I am extremely privileged to get
this all along the completion of my project. All that I have done is only due to
such supervision and assistance and I would not forget to thank them.

Firstly I would like to express my sincere gratitude to DR. ANIRUDH

PORVAL, P.G.T CHEMISTRY, GAYATRI VIDYAPEETH,
SHANTIKUNJ HARIDWAR, for inspiring me in choosing the most
appropriate and suitable project for me, continuous support for my project related
research, for his patience, motivation and immense knowledge. His guidance
helped me in all the time of research and writing of this thesis. I could not have
imagined having a better advisor and mentor for my project.

Secondly I am very thankful to MR. S. R. SINHA, PRINCIPAL, GAYATRI

VIDYAPEETH, SHANTIKUNJ HARIDWAR, for providing us the laboratory
facilities, guidance and support.

I am immensely thankful to my CLASSMATES for the stimulating discussions,

for the continuous support and help which he provided me to achieve the perfect
completion of investigatory project, and for all the fun we have had in the one
year.

Last but not the least, I would like to thank MY PARENTS for supporting me
spiritually throughout writing this these is and my life in general and providing
me the facilities of internet and gadgets so that I can prepare my project in a fine
way.

AISHWARYA NISHAD
 INTRODUCTION
Proteins are of great nutritional value and are directly involved in the chemical
processes essential for life. The importance of proteins was recognized by
chemists in the early 19th century, including Swedish chemist Jöns Jacob
Berzelius, who in 1838 coined the term protein, a word derived from the Greek
prōteios, meaning “holding first place.” Proteins are species-specific; that is, the
proteins of one species differ from those of another species. They are also organ-
specific; for instance, within a single organism, muscle proteins differ from those
of the brain and liver.

A protein molecule is very large compared with molecules of sugar or salt and
consists of many amino acids joined together to form long chains, much as beads
are arranged on a string. There are about 20 different amino acids that occur
naturally in proteins. Proteins of similar function have similar amino acid
composition and sequence. Although it is not yet possible to explain all of the
functions of a protein from its amino acid sequence, established correlations
between structure and function can be attributed to the properties of the amino
acids that compose proteins.

Plants can synthesize all of the amino acids; animals cannot, even though all of
them are essential for life. Plants can grow in a medium containing inorganic
nutrients that provide nitrogen, potassium, and other substances essential for
growth. They utilize the carbon-dioxide in the air during the process of
photosynthesis to form organic compounds such as carbohydrates. Animals,
however, must obtain organic nutrients from outside sources. Because the protein
content of most plants is low, very large amounts of plant material are required by
animals, such as ruminants (e.g., cows), that eat only plant material to meet their
amino acid requirements. Non ruminant animals, including humans, obtain
proteins principally from animals and their products—e.g., meat, milk, and eggs.
The seeds of legumes are increasingly being used to prepare inexpensive protein-
rich food the structure of the animal.

66 blood plasma. Muscles, for example, contain about 30 percent protein, the liver
20 to 30 percent, and red blood cells 30 percent. Higher percentages of protein
are found in hair, bones, and other organs and tissues with a low water content.
The quantity of free amino acids and peptides in animals is much smaller than the
amount of protein; protein molecules are produced in cells by the stepwise
alignment of amino acids and are released into the body fluids only after synthesis
is complete.

The high protein content of some organs does not mean that the importance of
proteins is related to their amount in an organism or tissue; on the contrary, some
of the most important proteins, such as enzymes and hormones, occur in
extremely small amounts. The importance of proteins is related principally to
their function. All enzymes identified thus far are proteins. Enzymes, which are
the catalysts of all metabolic reactions, enable an organism to build up the
chemical substances necessary for life—proteins, nucleic acids, carbohydrates,
and lipids—to convert them into other substances, and to degrade them. Life
without enzymes is not possible. There are several protein hormones with
important regulatory functions. In all vertebrates, the respiratory protein
hemoglobin acts as oxygen carrier in the blood, transporting oxygen from the
lung to body organs and tissues. A large group of structural proteins maintains
and protects body.

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

Proteins have a variety of function in cells. Major functions include acting as

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 expression, and so on. Enzymes are biological catalysts
that speed up a chemical reaction without being permanently altered. They have
“active sites” where the substrate/reactant binds, and they can be either activated
or inhibited (competitive and/or noncompetitive inhibitors).

Proteins are one of the most abundant organic molecules in living systems and
have the most diverse range of functions of all macromolecules. Proteins may be
structural, regulatory, contractile, or protective; they may serve in transport,
storage, or membranes; or they may be toxins or enzymes. Each cell in a living
system may contain thousands of proteins, each with a unique function. Their
structures, like their functions, vary greatly.
 AMINO ACID AS A BASIC UNIT OF
PROTEINS
The building blocks of proteins are amino acids, which are small organic
molecules that consist of an alpha (central) carbon atom linked to an amino group,
a carboxyl group, a hydrogen atom, and a variable component called a side chain
(see below). Within a protein, multiple amino acids are linked together by peptide
bonds, thereby forming a long chain. Peptide bonds are formed by a biochemical
reaction that extracts a water molecule as it joins the amino group of one amino
acid to the carboxyl group of a neighboring amino acid. The linear sequence of
amino acids within a protein is considered the primary structure of the protein.
Proteins are built from a set of only twenty amino acids, each of which has a
unique side chain. The side chains of amino acids have different chemistries. The
largest groups of amino acids have non polar side chains. Several other amino
acids have side chains with positive or negative charges, while others have polar
but uncharged side chains. The chemistry of amino acid side chains is critical to
protein structure because these side chains can bond with one another to hold a
length of protein in a certain shape or conformation. Charged amino acid side
chains can form ionic bonds, and polar amino acids are capable of forming
hydrogen bonds. Hydrophobic side chains interact with each other via weak van
der Waals interactions. The vast majority of bonds formed by these side chains
are non covalent. In fact, cysteines are the only amino acids capable of forming
covalent bonds, which they do with their particular side chains. Because of side
chain interactions, the sequence and location of amino acids in a particular protein
guides where the bends and folds occur in that protein
The primary structure of a protein — its amino acid sequence — drives the folding
and intra molecular bonding of the linear amino acid chain, which ultimately
determines the protein's unique three-dimensional shape. Hydrogen bonding
between amino groups and carboxyl groups in neighboring regions of the protein
chain sometimes causes certain patterns of folding to occur. Known as alpha
helices and beta sheets, these stable folding patterns make up the secondary
structure of a protein. Most proteins contain multiple helices and sheets, in
addition to other less common patterns (Figure 2). The ensemble of formations
and folds in a single linear chain of amino acids — sometimes called a
polypeptide — constitutes the tertiary structure of a protein. Finally, the
quaternary structure of a protein refers to those macromolecules with multiple
polypeptide chains or subunits.
The final shape adopted by a newly synthesized protein is typically the most
energetically favorable one. As proteins fold, they test a variety of conformations
before reaching their final form, which is unique and compact. Folded proteins
are stabilized by thousands of non-covalent bonds between amino acids. In
addition, chemical forces between a protein and its immediate environment
contribute to protein shape and stability. For example, the proteins that are
dissolved in the cell cytoplasm have hydrophilic (water-loving) chemical groups
on their surfaces, whereas their hydrophobic (water-averse) elements tend to be
tucked inside. In contrast, the proteins that are inserted into the cell membranes
display some hydrophobic chemical groups on their surface, specifically in those
regions where the protein surface is exposed to membrane lipids. It is important
to note, however, that fully folded proteins are not frozen into shape. Rather, the
atoms within these proteins remain capable of making small movements.

Even though proteins are considered macromolecules, they are too small to
visualize, even with a microscope. So, scientists must use indirect methods to
figure out what they look like and how they are folded. The most common method
used to study protein structures is X-ray crystallography. With this method,
solid crystals of purified protein are placed in an X-ray beam, and the pattern of
deflected X rays is used to predict the positions of the thousands of atoms within
the protein crystal.
 CLASSIFICATION OF PROTEINS
Protein classification based on shape

On the basis of their shape, proteins may be divided into two classes: fibrous and
globular.
Fibrous proteins

They have primarily mechanical and structural functions, providing support to

the cells as well as the whole organism.
These proteins are insoluble in water as they contain, both internally and on their
surface, many hydrophobic amino acids. The presence on their surface of
hydrophobic amino acids facilitates their packaging into very complex supra
molecular structures.
Some fibrous proteins, such as α-keratins, are only partially hydrolyzed in the
intestine.
Here are some examples.

Fibroin it is produced by spiders and insects. An example is that produced by the

silkworm, Bombyx mori.
Collagen
The term “collagen” indicates not a single protein but a family of structurally
related proteins (at least 29 different types), which constitute the main protein
component of connective tissue, and more generally, the extracellular scaffolding
of multi cellular organisms. In vertebrates, they represent about 2530% of all
proteins.
They are found in different tissues and organs, such as tendons and the organic
matrix of bone, where they are present in very high percentages, but also in
cartilage and in the cornea of the eye. In the different tissues, they form different
structures, each capable of satisfying a particular need. For example, in
the cornea, the molecules are arranged in an almost crystalline array, so that they
are virtually transparent, while in the skin they form fibers not very intertwined
and directed in all directions, which ensure the tensile strength of the skin itself.
Note: the different types of collagen have low nutritional value as deficient in
several amino acids (in fact, they contain no tryptophan and low amount of the
other essential amino acids). The gelatin used in food preparation is a derivative
of collagen.
α-Keratins
They constitute almost the entire dry weight of nails, claws, beak, hooves, horns, hair,
wool, and a large part of the outer layer of the skin.
The different stiffness and flexibility of these structures is a consequence of the
number of disulfide bonds that contribute, together with other binding forces, to
stabilize the protein structure. And this is the reason why wool keratins, which
have a low number of disulfide bonds, are flexible, soft and extensible, unlike
claw and beak keratins that are rich in disulfide bonds.

Elastin this protein provides elasticity to the skin and blood vessels, a
consequence of its random coiled structure that differs from the structures of the
α-keratins and collagens.
 Globular proteins

Most of the proteins belong to this class. They have a compact and more or less
spherical structure, more complex than fibrous proteins. In this regard, motifs,
domains, tertiary and quaternary structures are found, in addition to the secondary
structures. They are generally soluble in water but can also be found inserted into
biological membranes (Trans membrane proteins), thus in a hydrophobic
environment. Unlike fibrous proteins, that have structural and mechanical
functions, they act as:

• membrane transporters and receptors;

• transporters of triglycerides and fatty acids, two classes of lipids, and oxygen
in the blood;
• immunoglobulin or antibodies;
• Grain and legume storage proteins.
Examples of globular proteins are myoglobin, hemoglobin, and cytochrome c. At
the intestinal level, most of the globular proteins of animal origin are hydrolyzed
almost entirely to amino acids.

Protein classification based on biological functions

The multitude of functions that proteins perform is the consequence of both the
folding of the polypeptide chain, therefore of their three-dimensional structure,
and the presence of many different functional groups in the amino acid side
chains, such as thrills, alcohols, thioethers, carboxamides, carboxylic from the
functional point of view, they may be divided into several groups. In living
organisms, almost all reactions are catalyzed by specific proteins called enzymes.
They have a high catalytic power, increasing the rate of the reaction in which they
are involved at least by factor 106. Therefore, life as we

know could not exist without their “facilitating action”.

Almost all known enzymes, and in the human body they are thousand, are proteins
(except some catalytic RNA molecules called ribosome, that is, ribonucleic acid
enzymes).
Transport proteins many small molecules, organic and inorganic, are transported
in the bloodstream and extracellular fluids, across the cell membranes, and inside
the cells from one compartment to another, by specific proteins.
Examples are: hemoglobin, that carries oxygen from the alveolar blood vessels to
tissue capillaries; transferring, which carries iron in the blood; membrane carriers;
fatty acid binding proteins (FABP), that is, proteins of plasma lipoproteins,
macromolecular complexes of proteins and lipids responsible for the transport of
triglycerides, which are otherwise insoluble in water; albumin, that carries free
fatty acids, bilirubin, thyroid hormones, and certain medications such as aspirin
and penicillin, in the blood. Many of these proteins also play a protective role,
since the bound molecules, such as fatty acids, may be harmful for the organism
when present in free form.

• Storage proteins Examples are: ferritin, that stores iron intracellularly in a non-
toxic form; milk caseins, that act as a reserve of amino acids for the milk; egg
yolk phosvitin, that contains high amounts of phosphorus; prolamins and
glutelins, the storage proteins of cereals.
• Mechanical support Proteins has a pivotal role in the stabilization of many
structures. Examples are α-keratins, collagen and elastin. The same
cytoskeleton system, the scaffold of the cell, is made of proteins.
• They generate movement. They are responsible, among others, for: the
contraction of the muscle fibers (of which myosin is the main component); the
propulsion of spermatozoa and microorganisms with flagella; the separation of
chromosomes during mitosis.
• They are involved in nerve transmission. An example is the receptor for
acetylcholine at synapses.
• They control development and differentiation. Some proteins are involved in
the regulation of gene expression. An example is the nerve growth factor
(NGF), discovered by Rita Levi-Montalcini, that plays a leading role in the
formation of neural networks.
• They are regulatory molecules involved in the control of many cellular
functions, from metabolism to reproduction. Examples are insulin, glucagon,
and thyroid-stimulating hormone (TSH).
• The antibodies or immunoglobulin are glycoprotein’s that recognize antigens
expressed on the surface of viruses, bacteria and other infectious agents.

Interferon, fibrinogen, and factors of blood coagulation are other members of this
group.
Proteins, and in particular the amino acids that constitute them, act as energy
storage, second in size only to the adipose tissue, that in particular conditions,
such as prolonged fasting, may become essential for survival. However, their
reduction of more than 30% leads to a decrease of the contraction capacity of
respiratory muscle, immune function, and organ function that are not
compatible with life. Therefore, proteins are an extremely valuable fuel
 BIOLOGICAL ROLE OF PROTEINS
Proteins are molecules made of amino acids. They are coded for by our genes and
form the basis of living tissues. They also play a central role in biological
processes. For example, proteins catalyse reactions in our bodies, transport
molecules such as oxygen, keep us healthy as part of the immune system and
transmit messages from cell to cell.

Protein synthesis

A gene is a segment of a DNA molecule that contains the instructions needed to

make a unique protein. All of our cells contain the same DNA molecules, but each
cell uses a different combination of genes to build the particular proteins it needs
to perform its specialised functions.

Protein synthesis has 2 main stages. The 1st stage is known as transcription, where
a messenger molecule (mRNA) is formed. This molecule is transcribed from the
DNA molecule and carries a copy of the information needed to make a protein.
In the 2nd stage, the mRNA molecule leaves the nucleus for the cytoplasm where
the cell’s ribosomes read the information and start to assemble a protein in a
process called translation

During translation, the ribosomes read the mRNA sequence of bases 3 at a time.
These 3-letter combinations (called codons) each code a particular amino acid.
For example, the base sequence TTT codes for the amino acid lysine.

There are 4 bases (adenine, thymine, guanine and cytosine) and therefore 64 (43)
possible codons specified using some combination of 3 bases. However, only 20
amino acids are required to build all of the proteins in our bodies (some amino
acids are specified by more than 1 codon). It is the particular sequence of amino
acids that determines the shape and function of the protein.
Protein synthesis, like many other biological processes, can be affected by
environmental factors. These include maternal nutrition, temperature stress,
oxygen levels and exposure to chemicals

There are many different types of proteins in our bodies. They all serve important
roles in our growth, development and everyday functioning. Here are some
examples:

Enzymes are proteins that facilitate biochemical reactions, for example, pepsin is a
digestive enzyme in your stomach that helps to break down proteins in food.

Antibodies are proteins produced by the immune system to help remove foreign
substances and fight infections.

DNA-associated proteins regulate chromosome structure during cell division

and/or play a role in regulating gene expression, for example, histones and
cohesin proteins

Contractile proteins are involved in muscle contraction and movement, for example,
actin and myosin

Structural proteins provide support in our bodies, for example, the proteins in our
connective tissues, such as collagen and elastin.
Transport proteins move molecules around our bodies, for example, hemoglobin
transports oxygen through the blood.

DISORDERS OF PROTEINS
Dietary proteins are made of amino acids. The body can use dietary protein for
energy, muscle incorporation, or incorporation into nitrogen-containing
compounds.

Digestion of protein begins in the stomach with an enzyme called pepsin and
continues in the small intestine, where enzymes from the pancreas and intestinal
lining break the protein into smaller peptides. These peptides are then broken
down into tripeptides and dipeptides that can cross the intestinal lining.

Disorders of protein digestion can occur when any of these processes is altered or
abnormal.

At The Children's Hospital of Philadelphia, children with disorders of protein

digestion are managed by doctors in the Division of Gastroenterology (GI),
Hepatology and Nutrition
Diseases Involving Proteins
As you may recall, moderation refers to having the proper amount of a nutrient—
having neither too little nor too much. A healthy diet incorporates all nutrients in
moderation. Low protein intake has several health consequences, and a severe lack
of protein in the diet eventually causes death. Although severe protein deficiency
is a rare occurrence in children and adults in the United States, it is estimated that
more than half of the elderly in nursing homes are protein-deficient. The
Acceptable Macronutrient Distribution Range (AMDR) for protein for adults is
between 10 and 35 percent of kilocalories, which is a fairly wide range. The
percent of protein in the diet that is associated with malnutrition and its health
consequences is less than 10 percent, but this is often accompanied by deficiencies
in calories and other micronutrients. In this section we will discuss the health
consequences of protein intake that is either too low to support life’s processes or
too high, thereby increasing the risk of chronic
disease. In the last section of this chapter, we will discuss in more detail the
personal choices you can make to optimize your health by consuming the right
amount of high-quality protein.

Health Consequences of Protein Deficiency

Although severe protein deficiency is rare in the developed world, it is a leading
cause of death in children in many poor, underdeveloped countries. There are two
main syndromes associated with protein deficiencies: Kwashiorkor and
Marasmus. Kwashiorkor affects millions of children worldwide. When it was first
described in 1935, more than 90 percent of children with Kwashiorkor died.
Although the associated mortality is slightly lower now, most children still die
after the initiation of treatment. The name Kwashiorkor comes from a language
in Ghana and means, “rejected one.” The syndrome was named because it
occurred most commonly in children who had recently been weaned from the
breast, usually because another child had just been born. Subsequently the child
was fed watery porridge made from low-protein grains, which accounts for the
low protein intake. Kwashiorkor is characterized by swelling (edema) of the feet
and abdomen, poor skin health, growth retardation, low muscle mass and liver
malfunction. Recall that one of protein’s functional roles in the body is fluid
balance. Diets extremely low in protein do not provide enough amino acids for
the synthesis of albumin. One of the functions of albumin is to hold water in the
blood vessels, so having lower concentrations of blood albumin results in water
moving out of the blood vessels and into tissues, causing swelling. The primary
symptoms of Kwashiorkor include not only swelling, but also diarrhea, fatigue,
peeling skin, and irritability. Severe protein deficiency in addition to other
micronutrient deficiencies, such as folate (vitamin B9), iodine, iron, and vitamin
C all contribute to the many health manifestations of this syndrome.
Protein deficiency often leaves its mark on the skin, hair and nails, which are
largely made of protein.

For instance, kwashiorkor in children is distinguished by flaky or splitting skin,

redness and patches of depigmented skin

Hair thinning, faded hair color, hair loss (alopecia) and brittle nails are also
common symptoms

However, these symptoms are unlikely to appear unless you have a severe protein
deficiency.

Muscles are not the only tissues affected by low protein intake.

Your bones are also at risk. Not consuming enough protein may weaken your
bones and increase the risk of fractures

One study in postmenopausal women found that a higher protein intake was
associated with a lower risk of hip fractures. The highest intake was linked to a
69% reduced risk, and animal-source protein appeared to have the greatest
benefits

Another study in postmenopausal women with recent hip fractures showed that
taking 20 grams of protein supplements per day for half a year slowed bone loss
by 2.3%

CONCLUSION
Proteins are built as chains of amino acids, which then fold into unique
threedimensional shapes. Bonding within protein molecules helps stabilize their
structure, and the final folded forms of proteins are well-adapted for their
functions.
Protein is very important for almost all of the processes that occur in your body.
It is necessary for your body to make antibodies, which fight against infection
and illness, and protein is what keeps our hair, skin and bones healthy. Protein is
an important part of our daily diet and it should be consumed every day.
Nutritionists recommend that you eat 2-3 servings of dairy products every day
and 2-3 servings of meat, poultry, fish, or shellfish a day. They also suggested
that 10-35% of your calorie intake should be protein. Many nutritionists also
recommend an intake of 1 gram of protein per 1 kilogram of body weight.

Also too much protein damages the liver and kidneys. But protein helps your
body resist disease and infection. Protein is needed for the growth of your body.
Protein can help you lose weight, increase your metabolism and suppress your
appetite. Also women who are pregnant need protein for their fetus and to supply
breast milk. Without proteins, your body would lack the enzymes and hormones
you need for metabolism, digestion and other important processes. Your body
makes 11 of the amino acids but the 9 essential amino acids should be included
in your diet. If you eat an incomplete protein, you can make it a complete protein
by adding a small amount of animal products. Since most animal products are
high in calories and have fat, but are very rich in protein, don't forget you should
eat animal products in small moderations and make it in healthier ways.

Reference
https://www.michigan.gov/documents/explorelabscience/Introduction
_to_proteins_and_amino_acids_571576_7.pdf https://www.tuscany-
diet.net/proteins/classification/ https://www.chop.edu/conditions-
diseases/disorders-protein-digestion
https://www.sciencelearn.org.nz/resources/209-role-of-proteins-inthe-
body https://www.healthline.com/nutrition/protein-
deficiencysymptoms#TOC_TITLE_HDR_7