1

NAME: IKSHITA
SRIVASTAVA
CLASS: XII-G
CHEMISTRY
PROJECT
TOPIC: PROTEINS
SESSION: 2020-2021
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ACKNOWLEDGEME
NT
The city of Rome was not built in a day .Every
masterpiece requires continuous devotion ,creativity,
commitment and aspiration to make things perfect. This project
is based on the topic Proteins. I Ikshita Srivastava is highly
grateful to my Chemistry teacher respected Mr. Akhilesh Shukla
sir for enlightening me and motivating me to complete this
project and for providing an opportunity to learn various things
through this project. My experience in making this project was
awesome. It was a beautiful journey of knowledge and
enlightenment. A task always becomes easier if you have a
bunch of people behind to support and I thank each one of them
to make me gem on the diadem of wisdom.
I would also like to express my heartiest gratitude to my parents
for their support and immense co- operation .I would also like
to thank the Almighty God for bestowing his blessing upon me
and for helping me to make this project a success. I would also
like to express my heartiest thanks to all my friends who have
helped me with their valuable suggestions and guidance in
various phases of the completion of this project based on the
topic proteins and their role in lives.
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INDEX
s.no. TITLE SIGN

1. Introduction
2. Structure of Proteins
3. Functions of Proteins
4. Amino acids
5. Protein rich foods
6. Deproteination
7. DNA-Binding proteins
8. DNA-protein interactions
9. Conclusion

10. Bibliography
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INTRODUCTION
Protein is a macronutrient that is essential for building muscle mass. It
is commonly found in animal products, though it is also present in
other sources, such as nuts and legumes.
There are three macronutrients: protein, fats and carbohydrates.
Macronutrients provide calories, or energy. The body requires large
amounts of macronutrients to sustain life, hence the term “macro,”
according to the University of Illinois McKinley Health Centre. Each
gram of protein contains 4 calories. Protein makes up about 15 percent
of a person’s body weight.
Chemically, protein is composed of amino acids, which are organic
compounds made of carbon, hydrogen, nitrogen, oxygen or
sulphur .Amino acids are the building blocks of proteins, and proteins
are the building blocks of muscle mass, according to the National
Institutes of Health (NIH).
“When protein is broken down in the body it helps to fuel muscle mass,
which helps metabolism," said Jessica Crandall, a registered dietician
nutritionist, certified diabetes educator and national spokesperson for
the Academy of Nutrition and Dietetics. "It also helps the immune
system stay strong.”Moreover Proteins are large bio molecules,
or macromolecules, consisting of one or more long chains of amino
acid residues. Proteins perform a vast array of functions within
organisms, including catalysing metabolic reactions, DNA
replication, responding to stimuli, providing structure to cells,
and organisms, and transporting molecules from one location to
another. Proteins differ from one another primarily in their sequence of
amino acids, which is dictated by the nucleotide sequence of
their genes, and which usually results in protein folding into a
specific 3D structure that determines its activity.
A linear chain of amino acid residues is called a polypeptide. A
protein contains at least one long polypeptide. Short polypeptides,
containing less than 20–30 residues, are rarely considered to be
proteins and are commonly called peptides, or
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sometimes oligopeptides. The individual amino acid residues are

bonded together by peptide bonds and adjacent amino acid residues.
The sequence of amino acid residues in a protein is defined by
the sequence of a gene, which is encoded in the genetic code. In
general, the genetic code specifies 20 standard amino acids; but in
certain organisms the genetic code can include selenocysteine and—in
certain archaea—pyrrolysine. Shortly after or even during synthesis,
the residues in a protein are often chemically modified by post-
translational modification, which alters the physical and chemical
properties, folding, stability, activity, and ultimately, the function of the
proteins. Some proteins have non-peptide groups attached, which can
be called prosthetic groups or cofactors. Proteins can also work
together to achieve a particular function, and they often associate to
form stable protein complexes.
Once formed, proteins only exist for a certain period and are
then degraded and recycled by the cell's machinery through the process
of protein turnover. A protein's lifespan is measured in terms of
its half-life and covers a wide range. They can exist for minutes or
years with an average lifespan of 1–2 days in mammalian cells.
Abnormal or misfiled proteins are degraded more rapidly either due to
being targeted for destruction or due to being unstable.
HISTORY AND ETYMOLOGY OF PROTEINS:
Proteins were recognized as a distinct class of biological molecules in
the eighteenth century by Antoine Fourcroy and others, distinguished
by the molecules' ability to coagulate or flocculate under treatments
with heat or acid .Noted examples at the time included albumin
from egg whites, blood serum albumin, fibrin, and wheat gluten.
Proteins were first described by the Dutch chemist Gerardus Johannes
Mulder and named by the Swedish chemist Jöns Jacob Berzelius in
1838.Mulder carried out elemental analysis of common proteins and
found that nearly all proteins had the same empirical formula,
C400H620N100O120P1S1 He came to the erroneous conclusion that they
might be composed of a single type of (very large) molecule. The term
"protein" to describe these molecules was proposed by Mulder's
associate Berzelius. Protein is derived from the Greek word (proteios),
meaning "primary", "in the lead", or "standing in front".Prior to
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"protein", other names were used, like "albumins" or "albuminous

materials"

ATOMIC STRUCTURE OF PROTEIN

Early nutritional scientists such as the German Carl von Voit believed

that protein was the most important nutrient for maintaining the
structure of the body, because it was generally believed that "flesh
makes flesh." Karl Heinrich Ritthausen extended known protein forms
with the identification of glutamic acid. At the Connecticut
Agricultural Experiment Station a detailed review of the vegetable
proteins was compiled by Thomas Burr Osborne. Working
with Lafayette Mendel and applying Liebig's law of the minimum in
feeding laboratory rats, the nutritionally essential amino acids were
established. The work was continued and communicated by William
Cumming Rose. The understanding of proteins as polypeptides came
through the work of Franz Hofmeister and Hermann Emil Fischer in
1902. The central role of proteins as enzymes in living organisms was
not fully appreciated until 1926, when James B. Sumner showed that
the enzyme urease was in fact a protein.
The difficulty in purifying proteins in large quantities made them very
difficult for early protein biochemists to study. Hence, early studies
focused on proteins that could be purified in large quantities, e.g., those
of blood, egg white, various toxins, and digestive/metabolic enzymes
obtained from slaughterhouses.
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Linus Pauling is credited with the successful prediction of regular

protein secondary structures based on hydrogen bonding, an idea first
put forth by William Astbury in 1933.
The first protein to be sequenced was insulin, by Frederick Sanger, in
1949. Sanger correctly determined the amino acid sequence of insulin,
thus conclusively demonstrating that proteins consisted of linear
polymers of amino acids rather than branched chains, colloids,
or cyclols. He won the Nobel Prize for this achievement in 1958.
The first protein structures to be solved
were haemoglobin and myoglobin, by Max Perutz and Sir John
Cowdery Kendrew, respectively, in 1958.

Constituent amino-acids can be analyzed to predict secondary, tertiary

and quaternary protein structure, in this case haemoglobin
containing heme units.
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STRUCTURE OF
PROTEINS
Proteins are a polymeric chain of amino acid residues. The structure of
a protein is mainly composed of long chains of amino acids. The
structure and position of amino acids give particular properties to the
proteins. Amino acids are made up of an amino functional group (-
NH2) and a carboxyl group (-COOH).
Amino acids are linked together to form polypeptide chains. One or
several of such chains fold differently to form a protein. Amino acids
are substituted methane, where the four valencies of the α- carbon
are occupied by hydrogen, amino group, carboxyl group, and the fourth
valency is fulfilled by a variable R- group.
Depending on the R-group, there are different types of amino acids, out
of which 20 are found in a polypeptide chain. All these properties of
amino acids decide the ultimate structure and function of proteins.
The structure of the protein is classified at 4 levels:-

 Primary – The primary structure of a protein is the linear

polypeptide chain formed by the amino acids in a particular
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sequence. Changing the position of even a single amino acid will

result in a different chain and hence a different protein.
 Secondary – The secondary structure of a protein is formed by
hydrogen bonding in the polypeptide chain. These bonds cause
the chain to fold and coil in two different conformations known
as the α-helix or β-pleated sheets. The α-helix is like a single
spiral and is formed by hydrogen bonding between every fourth
amino acid. The β-pleated sheet is formed by hydrogen bonding
between two or more adjacent polypeptide chains.
 Tertiary – The tertiary structure is the final 3-dimensional shape
acquired by the polypeptide chains under the attractive and
repulsive forces of the different R-groups of each amino acid.
This is a coiled structure that is very necessary for protein
functions.
 Quaternary – This structure is exhibited only by those proteins
which have multiple polypeptide chains combined to form a large
complex. The individual chains are then called subunits.

Here are 9 important functions of proteins:

FUNCTIONS OF
PROTEINS
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Proteins are a class of macromolecules that perform a diverse range of

functions for the cell. They help in metabolism by providing structural
support and by acting as enzymes, carriers, or hormones. The building
blocks of proteins (monomers) are amino acids. Each amino acid has a
central carbon that is linked to an amino group, a carboxyl group, a
hydrogen atom, and an R group or side chain. There are 20 commonly
occurring amino acids, each of which differs in the R group. Each
amino acid is linked to its neighbours by a peptide bond. A long chain
of amino acids is known as a polypeptide.
Proteins are organized at four levels: primary, secondary, tertiary, and
(optional) quaternary. The primary structure is the unique sequence of
amino acids. The local folding of the polypeptide to form structures
such as the α helix and β-pleated sheet constitutes the secondary
structure. The overall three-dimensional structure is the tertiary
structure. When two or more polypeptides combine to form the
complete protein structure, the configuration is known as the
quaternary structure of a protein. Protein shape and function are
intricately linked; any change in shape caused by changes in
temperature or pH may lead to protein denaturation and a loss in
function.

1. Growth and Maintenance:

Your body needs protein for growth and maintenance of tissues.

Yet, your body’s proteins are in a constant state of turnover.

Under normal circumstances, your body breaks down the same amount
of protein that it uses to build and repair tissues. Other times, it breaks
down more protein than it can create, thus increasing your body’s
needs.

This typically happens in periods of illness, during pregnancy and

while breastfeeding .

People recovering from an injury or surgery, older adults and athletes

require more protein as well .
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Protein is required for the growth and maintenance of tissues. Your

body’s protein needs are dependent upon your health and activity level.

2. Causes Biochemical Reactions:

Enzymes are proteins that aid the thousands of biochemical reactions
that take place within and outside of your cells.

The structure of enzymes allows them to combine with other molecules

inside the cell called substrates, which catalyze reactions that are
essential to your metabolism.

Enzymes may also function outside the cell, such as digestive

enzymes like lactose and sucrose, which help digest sugar.

Some enzymes require other molecules, such as vitamins or minerals,

for a reaction to take place.

Bodily functions that depend on enzymes include:

 Digestion
 Energy production
 Blood clotting
 Muscle contraction

Lack or improper function of these enzymes can result in disease.

Enzymes are proteins that allow key chemical reactions to take place
within your body.

3. Acts as a Messenger:
Some proteins are hormones, which are chemical messengers that aid
communication between your cells, tissues and organs.
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They’re made and secreted by endocrine tissues or glands and then

transported in your blood to their target tissues or organs where they
bind to protein receptors on the cell surface.

Hormones can be grouped into three main categories :

 Protein and peptides: These are made from chains of amino

acids, ranging from a few to several hundred.
 Steroids: These are made from the fat cholesterol. The sex
hormones, testosterone and oestrogen, are steroid-based.
 Amines: These are made from the individual amino acids
tryptophan or tyrosine, which help make hormones related to
sleep and metabolism.

Protein and polypeptides make up most of your body’s hormones.

Some examples include :

 Insulin: Signals the uptake of glucose or sugar into the cell.

 Glucagon: Signals the breakdown of stored glucose in the liver.
 HGH (human growth hormone): Stimulates the growth of
various tissues, including bone.
 ADH (antidiuretic hormone): Signals the kidneys to reabsorb
water.
 ACTH (adrenocorticotropic hormone): Stimulates the release
of cortisol, a key factor in metabolism.
Amino acid chains of various lengths form protein and peptides, which
make up several of your body’s hormones and transmit information
between your cells, tissues and organs.

4. Provides Structure:
Some proteins are fibrous and provide cells and tissues with stiffness
and rigidity.
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These proteins include keratin, collagen and elastin, which help form

the connective framework of certain structures in your body.

Keratin is a structural protein that is found in your skin, hair and nails.

Collagen is the most abundant protein in your body and is the structural
protein of your bones, tendons, ligaments and skin .

Elastin is several hundred times more flexible than collagen. Its high
elasticity allows many tissues in your body to return to their original
shape after stretching or contracting, such as your uterus, lungs and
arteries.

A class of proteins known as fibrous proteins provide various parts of

your body with structure, strength and elasticity.

5. Maintains Proper Ph:

Protein plays a vital role in regulating the concentrations of acids and
bases in your blood and other bodily fluids.

The balance between acids and bases is measured using the pH scale. It
ranges from 0 to 14, with 0 being the most acidic, 7 neutral and 14 the
most alkaline.

Examples of the pH value of common substances include:

 pH 2: Stomach acid
 pH 4: Tomato juice
 pH 5: Black coffee
 pH 7.4: Human blood
 pH 10: Milk of magnesia
 pH 12: Soapy water

A variety of buffering systems allows your bodily fluids to maintain

normal pH ranges.
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A constant pH is necessary, as even a slight change in pH can be

harmful or potentially deadly.

One way your body regulates pH is with proteins. An example is

haemoglobin, a protein that makes up red blood cells.

Haemoglobin binds small amounts of acid, helping to maintain the

normal pH value of your blood.

The other buffer systems in your body include phosphate and

bicarbonate .

Proteins act as a buffer system, helping your body maintain proper pH

values of the blood and other bodily fluids.

6. Balances Fluids:
Proteins regulate body processes to maintain fluid balance.

Albumin and globulin are proteins in your blood that help maintain
your body’s fluid balance by attracting and retaining water .

If you don’t eat enough protein, your levels of albumin and globulin
eventually decrease.

Consequently, these proteins can no longer keep blood in your blood

vessels, and the fluid is forced into the spaces between your cells.

As the fluid continues to build up in the spaces between your cells,

swelling or oedema occurs, particularly in the stomach region.

This is a form of severe protein malnutrition called kwashiorkor that

develops when a person is consuming enough calories but does not
consume enough protein .

Kwashiorkor is rare in developed regions of the world and occurs more

often in areas of starvation.
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Proteins in your blood maintain the fluid balance between your blood
and the surrounding tissues.

7. Bolsters Immune Health:

Proteins help form immunoglobulin, or antibodies, to fight infection.

Antibodies are proteins in your blood that help protect your body from
harmful invaders like bacteria and viruses.

When these foreign invaders enter your cells, your body produces
antibodies that tag them for elimination.

Without these antibodies, bacteria and viruses would be free to

multiply and overwhelm your body with the disease they cause.

Once your body has produced antibodies against a particular bacteria or

virus, your cells never forget how to make them.

This allows the antibodies to respond quickly the next time a particular
disease agent invades your body.

As a result, your body develops immunity against the diseases to which

it is exposed .

Proteins form antibodies to protect your body from foreign invaders,

such as disease-causing bacteria and viruses.

8. Transports and Stores Nutrients:

Transport proteins carry substances throughout your bloodstream —
into cells, out of cells or within cells.

The substances transported by these proteins include nutrients like

vitamins or minerals, blood sugar, cholesterol and oxygen.
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For example, haemoglobin is a protein that carries oxygen from your

lungs to body tissues. Glucose transporters (GLUT) move glucose to
your cells, while lipoproteins transport cholesterol and other fats in
your blood.

Protein transporters are specific, meaning they will only bind to

specific substances. In other words, a protein transporter that moves
glucose will not move cholesterol.

Proteins also have storage roles. Ferritin is a storage protein that stores
iron .

Another storage protein is casein, which is the principal protein in milk

that helps babies grow.

Some proteins transport nutrients throughout your entire body, while

others store them.

9. Provides Energy:
Proteins can supply your body with energy.

Protein contains four calories per gram, the same amount of energy that
carbohydrates provide. Fats supply the most energy, at nine calories per
gram.

However, the last thing your body wants to use for energy is protein
since this valuable nutrient is widely used throughout your body.

Carbohydrates and fats are much better suited for providing energy, as
your body maintains reserves for use as fuel. Moreover, they’re
metabolized more efficiently compared to protein .

In fact, protein supplies your body with very little of its energy needs
under normal circumstances.
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However, in a state of fasting (18–48 hours of no food intake), your

body breaks down skeletal muscle so that the amino acids can supply
you with energy.

Your body also uses amino acids from broken-down skeletal muscle if
carbohydrate storage is low. This can occur after exhaustive exercise or
if you don’t consume enough calories in general .

Protein can serve as a valuable energy source but only in situations of

fasting, exhaustive exercise or inadequate calorie intake

AMINO ACIDS:
Amino acids are the monomers that make up proteins. Specifically, a
protein is made up of one or more linear chains of amino acids, each of
which is called a polypeptide. (We'll see where this name comes from
a little further down the page.) There are 202020 types of amino acids
commonly found in proteins.

Amino acid structure

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Image of an amino acid, indicating the amino group, carboxyl group,

alpha carbon, and R group.

Amino acids share a basic structure, which consists of a central carbon

atom, also known as the alpha (α) carbon, bonded to an amino group
2NH2start a carboxyl group COOH start text, C, O, O, H, end text),
and a hydrogen atom.
Although the generalized amino acid shown above is shown with its
amino and carboxyl groups neutral for simplicity, this is not actually
the state in which an amino acid would typically be found. At
physiological pH (7.27.27, point, 2 - 7.47.47, point, 4), the amino
group is typically protonated and bears a positive charge, while the
carboxyl group is typically deprotonated and bears a negative charge.
Every amino acid also has another atom or group of atoms bonded to
the central atom, known as the R group, which determines the identity
of the amino acid. For instance, if the R group is a hydrogen atom, then
the amino acid is glycine, while if it’s a methyl group, the amino acid is
alanine.
There are two main categories of amino acids in the body. First, we’ve
got essential amino acids – those that the body can’t manufacture, and
thus we must consume in our diets.
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Some amino acids are conditionally essential, which means that our
bodies can’t always make as much as we need (for example, when
we’re under stress).
Next we have got nonessential amino acids – those that the body can
usually make for itself.
CLASSIFICATION OF AMINO ACID ON THE BASIS
OF NUTRITION:
Essential amino acids Conditionally essential Non essential amino acids
amino acids
Histidine Arginine Alanine
Isoleucine Cysteine Asparagine
Leucine Glutamine Aspartic acid
Lysine Tyrosine Glutamic acid
Methionine Proline
Phenylalanine Serine
Threonine
Tryptophan
Valine
CLASSIFICATION OF AMINO ACID ON THE BASIS
OF RELATIVE NUMBER OF –NH2 –COOH GROUPS:
 NEUTRAL AMINO ACIDS: The amino acids containing
one –NH2 group and one –COOH group are called neutral amino
acids. For example: glycine ,valine,alanine etc are the amino
acids of this type.
 ACIDIC AMINIO ACIDS: The amino acids containing two
–COOH groups and one –NH2 group are called acidic amino
acids. For example :aspartic acid, glutamic acid, etc are acidic
amino acids.
 BASIC AMINO ACIDS: The amino acids containing two –
NH2 groups and one –COOH group are called basic amino
acids.Some examples of basic amino acids are lysine, arginine
etc.
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PHYSICAL PROPERTY OF ALPHA AMINO

ACIDS:

 Each amino acid has both an acidic and basic group as you can
see from its structure. This is the reason they behave like salts.
 Any amino acid in the dry state is in crystalline form. They exist
as a dipolar ion. The COOH group exists as an anion. And the
NH2 group exists as a cation. This dipolar ion has a special
name “Zwitter ion”
 In aqueous solution, alpha amino acids exist
in equilibrium between a cationic form, an anionic form and
dipolar ion.
 The Isoelectric point is the pH point at which the concentration of
zwitter ions is the highest ad the concentration of cationic and
anionic form is equal. This point is definite for every α-amino
acid.
 They are generally water soluble and also have high melting
points.
FORMATION OF ZWITTER ION (INTERNAL SALT):
A zwitter ion is a molecule that has at least two functional groups: one
having a positive charge and the other having a negative charge, with
an overall charge of zero.
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 ISOELECTRIC POINT:

The isoelectric point (pI, pH(I), IEP), is the pH at which

a molecule carries no net electrical charge or is electrically neutral in
the statistical mean. The standard nomenclature to represent the
isoelectric point is pH(I). However, pI is also used. For brevity, this
article uses pI. The net charge on the molecule is affected by pH of its
surrounding environment and can become more positively or
negatively charged due to the gain or loss, respectively,
of protons (H+).
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 CHEMICAL PROPERTIES OF ALPHA AMINO

ACIDS:
The chemical properties of alpha amino acids are similar to those
of primary amines and carboxylic acids. They form salts with
acids as well as with bases.
PEPTIDES AND PEPTIDE BOND:
 A peptide is a short-chain made up of amino acid which, together
with other peptides, forms a protein.
 The number of amino acids in a peptide can range from two
amino acids to fifty amino acids.
 Based on the number of amino acids present in the peptide,
peptides are of many types; peptides with ten or fewer amino
acids are termed oligopeptides, and the peptides with more than
ten amino acids are termed polypeptides.
 Polypeptides with around 100 amino acids are then considered
proteins.
 A peptide bond is a special type of amide bond formed between
two molecules where an α-carboxyl group of one molecule reacts
with the α-amino group of another molecule releasing a water
molecule.
 The peptide bond is also referred to as the isopeptide bond where
the amide bond forms between the carboxyl group of one amino
acid and the amino group of another amino acid at other positions
than the alpha.
 The process of formation of the peptide bond is an example of a
condensation reaction resulting in dehydration (removal of
water).
 Peptide bonds are covalent bonds that exist between any two
amino acids resulting in a peptide chain.
 A partial double bond exists between carbon and nitrogen of the
amide bond which stabilizes the peptide bond.
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PROTEINS AND POLYPEPTIDES

Polypeptides help make up proteins by bonding numerous amino acids

together. Proteins are created by the bonding of two or more
polypeptides, which are then folded into a specific shape for a
particular protein.

CLASSIFICATION OF PROTEINS:
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Classification of proteins is done on the basis of the following:

 Shape
 Constitution
 Nature of molecules
On the basis of shape

 Fibrous protein(Scleroprotein): We can find these proteins in

animals and are insoluble in water. Fibrous proteins are resistant to
proteolytic enzymes and are coiled and exist in threadlike structures
to form fibres. e.g. collagen, actin, and myosin, keratin in hair,
claws, feathers, etc.
 Globular proteins: These proteins, unlike fibrous proteins are
soluble in water. They are made up of polypeptides that are coiled
about themselves to form oval or spherical molecules e.g. albumin,
insulin, and hormones like oxytocin, etc.
On the basis of Constitution

 Simple proteins: These proteins are made up of amino acids only.

e.g. albumins, globulins, prolamins, etc.
 Conjugated proteins: These are complex proteins that are
combined with the characteristic of non–amino acid substance called
as a prosthetic group. These are of following types:–
o Nucleoproteins: Combination of protein and nucleic acid
o Mucoproteins: Combination of proteins and carbohydrates (>4%)
o Glycoproteins: Combination of proteins and carbohydrates(<4%)
o Chromoproteins: Combination of proteins and coloured pigments.
o Lipoproteins: Combination of proteins and lipids.
o Metalloprotein: Combination of proteins and metal ions.
o Phosphoprotein: Combination of proteins and phosphate group.
 25

 Derived proteins: When proteins are hydrolyzed by acids, alkalies

or enzymes, the degradation products obtained from them are called
derived proteins.
On the basis of nature of Molecules

 Acidic proteins: They exist as anion and contain acidic amino acids.

e.g. blood groups.
 Basic proteins: They exist as cations and are rich in basic amino
acids e.g. lysine, arginine etc.

PROTEIN RICH FOODS:

1. Eggs:
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Whole eggs are among the healthiest and most nutritious foods
available.

They’re an excellent source of proteins and eye-protecting

antioxidants, and help in growth and development of the body as a
whole.

Whole eggs are high in protein, but egg whites are almost pure protein.

Egg and foods containing egg are not suitable for people with an egg
allergy.

Protein content: 33% of calories in a whole egg. One large egg has 6

grams of protein and 78 calories.

2. Almonds:
 27

Almonds are a popular type of tree nut.

They are rich in essential nutrients, including fiber, vitamin E,

manganese, and magnesium.

Almonds are not suitable for people who have a nut allergy.

Protein content: 15% of calories. 6 grams and 164 calories per ounce

(28 grams).

Other high protein rich nuts:

Pistachios  (13% of calories) and cashews (11% of calories).

3.Milk:
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Milk contains a little of nearly every nutrient that your body needs.

It’s a good source of high quality protein, and it’s high in calcium,
phosphorus, and riboflavin (vitamin B2).

If you are concerned about your fat intake, low or zero fat milk is an
option.

For those with lactose intolerance, consuming milk can lead to

gastrointestinal symptoms. People with a milk allergy can likewise
experience severe symptoms, so dairy milk is not a suitable option for
them either.

For those who wish to drink milk but either cannot tolerate it or follow
a purely plant-based diet, alternatives include soy milk.

Protein content: 21% of calories. One cup of whole milk contains 8

grams of protein and 149 calories. One cup of soy milk contains 6.3
grams of protein and 105 calories.
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PROTEIN DEFICIENCY:
The term ‘protein deficiency’ represents a state of relative or absolute
deficiency of body proteins or one or more of the essential amino acids.
‘Protein turnover’ reflects the balance of protein degradation and
resynthesis. More synthesis than breakdown indicates an anabolic state
that builds lean tissues, more breakdown than synthesis indicates a
catabolic state that burns lean tissues. The quantitative relationship
between circulating amino acid concentrations and their rate
of catabolism is not uniform, either between individuals or between
diets. A persistently high or low intake of protein leads to an overall
increase or decrease in rate of amino acid catabolism that is partially
independent of circulating amino acid concentrations. Although the
main cause of protein deficiency is a protein-deficient diet, the disorder
can commonly occur in a variety of pathologic states. The dietary
treatment of protein deficiency depends on the cause of the deficiency
and must depend on a sound understanding of the underlying disorder
and the mainstay of treatment includes balanced energy-protein
and micronutrient supplementation.

If a person does not consume enough protein, they may experience:

 lack of growth
 loss of muscle mass
 reduced immunity
 weakening of the heart
 respiratory problems
 30

A protein deficiency can be fatal. In developing countries, some people

develop kwashiorkor as a result of protein deficiency. It is a type
of malnutrition, and it is common during a famine.

Early signs include swelling in the legs and possibly the face, due

to edema, or fluid collecting under the skin. Other symptoms are a pot
belly, fatigue, dry brittle hair, and cracked nails. The person will be
more prone to infections.

In developed countries, those most at risk of a protein deficiency

include people who do not eat properly, for example, due to a poorly
managed weight loss diet, an eating disorder, or inability to cook their
own food, for example, in older age.

Most Americans do not lack protein in their diet.

IMPORTANCE OF GETTING ENOUGH PROTEIN:

During digestion, the body breaks down the protein we eat into
individual amino acids, which contribute to the plasma pool of amino
acids. This pool is a storage reserve of amino acids that circulate in the
blood.
The amino acid pool in the bloodstream readily trades with the amino
acids and proteins in our cells, provides a supply of amino acids as
needed, and is continuously replenished.
Since our bodies need proteins and amino acids to produce important
molecules in our body – like enzymes, hormones, neurotransmitters,
and antibodies – without an adequate protein intake, our bodies can’t
function well at all.
Protein helps replace worn out cells, transports various substances
throughout the body, and aids in growth and repair.
Consuming protein can also increase levels of the hormone glucagon,
and glucagon can help to control body fat.1 Glucagon is released when
blood sugar levels go down.  This causes the liver to break down stored
glycogen into glucose for the body.

It can also help to liberate free fatty acids from adipose tissue – another
way to get fuel for cells.
 31

HOW MUCH PROTEIN DO WE NEED?

How much protein you need depends on a few factors, but one of the
most important is your activity level.
The basic recommendation for protein intake is 0.8 grams per kilogram
(or around 0.36 g per pound) of body mass in untrained, generally
healthy adults. For instance, a 150 lb (68 kg) person would consume
around 54 grams a day.
However, this amount is only to prevent protein deficiency. It’s not
necessarily optimal, particularly for people such as athletes who train
regularly and hard.
For people doing high intensity training, protein needs might go up to
about 1.4-2.0 g/kg (or around 0.64-0.9 g/lb) of body mass.Our
hypothetical 150 lb (68 kg) person would thus need about 95-135 g of
protein per day.

Deproteination

Deproteination is the process of eliminating protein from some live

materials. This procedure is particularly common in studies on the
inorganic part of bone, teeth and shells.
Several different methods can be used for deproteination, such as the
method that uses hydrazine, the method that uses NaOH and the
method that uses enzymes.

DNA-binding proteins :
 32

DNA-binding proteins are proteins that have DNA-binding

domains and thus have a specific or general affinity for single- or
double-stranded DNA. Sequence-specific DNA-binding proteins
generally interact with the major groove of B-DNA, because it exposes
more functional groups that identify a base pair. However, there are
some known minor groove DNA-binding ligands such
as netropsin, distamycin, pentamidine, DAPI and others.

DNA-binding proteins include transcription factors which modulate the
process of transcription, various polymerases, nucleases which cleave
DNA molecules, and histones which are involved
in chromosome packaging and transcription in the cell nucleus. DNA-
binding proteins can incorporate such domains as the zinc finger,
the helix-turn-helix, and the leucine zipper (among many others) that
facilitate binding to nucleic acid.

Non-specific DNA-protein interactions:

 33

Structural proteins that bind DNA are well-understood examples of

non-specific DNA-protein interactions. Within chromosomes, DNA is
held in complexes with structural proteins. These proteins organize the
DNA into a compact structure called chromatin. In eukaryotes, this
structure involves DNA binding to a complex of small basic proteins
called histones. In prokaryotes, multiple types of proteins are involved. 

Pro
teins that specifically bind single-stranded DNA
A distinct group of DNA-binding proteins are the DNA-binding
proteins that specifically bind single-stranded DNA. In
humans, replication protein A is the best-understood member of this
family and is used in processes where the double helix is separated,
including DNA replication, recombination and DNA repair. These
binding proteins seem to stabilize single-stranded DNA and protect it
from forming stem-loops or being degraded by nucleases.

Protein–DNA interactions
Protein–DNA interactions occur when a protein binds a molecule
of DNA, often to regulate the biological function of DNA, usually
the expression of a gene. Among the proteins that bind to DNA
are transcription factors that activate or repress gene expression by
binding to DNA motifs and histones that form part of the structure of
DNA and bind to it less specifically. Also proteins that repair
DNA such as uracil-DNA glycosylase interact closely with it.
 34

In general, proteins bind to DNA in the major groove; however, there

are exceptions. Protein–DNA interaction are of mainly two types,
either specific interaction, or non-specific interaction. Recent single-
molecule experiments showed that DNA binding proteins undergo of
rapid rebinding in order to bind in correct orientation for recognizing
the target site.
Protein Data Bank (PDB):
The Protein Data Bank (PDB)  is a database for the three-dimensional
structural data of large biological molecules, such
as proteins and nucleic acids.The PDB is overseen by an organization
called the Worldwide Protein Data Bank, wwPDB.
The PDB is a key in areas of structural biology, such as structural
genomics. Most major scientific journals, and some funding agencies,
now require scientists to submit their structure data to the PDB. Many
other databases use protein structures deposited in the PDB. For
example, SCOP and CATH classify protein structures.
 35

CONCLUSION
 Proteins are built as chains of amino acids, which then fold into
unique three-dimensional shapes. Bonding within protein molecules
helps stabilize their structure, and the final folded forms of proteins are
well-adapted for their functions.

All proteins bind to other molecules in order to complete their tasks,

and the precise function of a protein depends on the way its exposed
surfaces interact with those molecules. Proteins with related shapes
tend to interact with certain molecules in similar ways, and these
proteins are therefore considered a protein family. The proteins within
a particular family tend to perform similar functions within the cell.
Proteins from the same family also often have long stretches of similar
amino acid sequences within their primary structure. These stretches
have been conserved through evolution and are vital to the catalytic
function of the protein. For example, cell receptor proteins contain
different amino acid sequences at their binding sites, which receive
chemical signals from outside the cell, but they are more similar in
amino acid sequences that interact with common intracellular signaling
proteins. Protein families may have many members, and they likely
evolved from ancient gene duplications. These duplications led to
modifications of protein functions and expanded the functional
repertoire of organisms over time.
 36

BIBLIOGRAPHY
The contextual facts have been taken from newspapers and magazines
related to the biological development in the cosmos.
I have gathered the material from the following websites:
 www.wikipedia.com
 www.proteinpedia.com
 www.nature.co.in
 www.openedu.com