9 Important Functions of Protein in Your Body

Protein is crucial to good health.

In fact, the name comes from the Greek word proteos, meaning “primary” or “first place.”

Proteins are made up of amino acids that join together to form long chains. You can think of a protein as a
string of beads in which each bead is an amino acid.

There are 20 amino acids that help form the thousands of different proteins in your body.

Proteins do most of their work in the cell and perform various jobs.

Here are 9 important functions of protein in your body.

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.

SUMMARY

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 lactase and sucrase, 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.

SUMMARY

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.

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 (11):

 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 estrogen, 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.

SUMMARY

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.

These proteins include keratin, collagen and elastin, which help form the connective framework of certain
structures in your body (13).

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 (14).

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 (15).

SUMMARY

A class of protein known as fibrous protein provides 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.

A constant pH is necessary, as even a slight change in pH can be harmful or potentially deadly (19, 20).

One way your body regulates pH is with proteins. An example is hemoglobin, a protein that makes up red
blood cells.

Hemoglobin 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.

SUMMARY

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 edema 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.

SUMMARYProteins in your blood maintain the fluid balance between your blood and the surrounding
tissues.

7. Bolsters Immune Health

Proteins help form immunoglobulins, 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.

SUMMARY
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.

For example, hemoglobin 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.

SUMMARY

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 carbs 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.

Carbs 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.

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.

SUMMARY

Protein can serve as a valuable energy source but only in situations of fasting, exhaustive exercise or
inadequate calorie intake.
 The Bottom Line

Protein has many roles in your body.

It helps repair and build your body’s tissues, allows metabolic reactions to take place and coordinates
bodily functions.

In addition to providing your body with a structural framework, proteins also maintain proper pH and
fluid balance.

Finally, they keep your immune system strong, transport and store nutrients and can act as an energy
source, if needed.

Collectively, these functions make protein one of the most important nutrients for your health.

Proteins

Proteins are important molecules in cells. Proteins are the major component of the dry weight of cells.
The name protein is derived from a Greek word Proteios which means pre-eminent or first. This name
was fist suggested in 1838 by a Swedish chemist Berzelius. He suggested it to a Dutch chemist Mulder
and he referred it to the complex organic substances found in the cells of living beings.
Proteins are the most abundant intracellular macro-molecules. Proteins are connected intimately with all
chemical and physical activity, which constitutes the life of the cell. Proteins are present in and vital to all
living cells. They provide structure, protection to the body of multicellular organism in the form of skin,
hair, callus, cartilage, ligaments, muscles, tendons. Proteins regulate and catalyze the body chemistry in
the form of hormones, enzymes, immunoglobulins etc.

What are Proteins?

Proteins are known as building blocks of life. Proteins are biomolecules, usually large in size, that
consists of one or more chains of amino acids. Proteins perform variety of functions like catalyzing
metabolic reactions, replication of DNA, response to stimuli, and transporting molecules. Proteins differ
from each other mainly in the sequences of amino acids.

Characteristics of Proteins

General Characteristics of Proteins are as follows:

 Proteins are organic substances; they are made up of nitrogen and also, oxygen, carbon and
hydrogen.

 Proteins are the most important biomolecules, they are the fundamental constituent of the
cytoplasm of the cell.

 Proteins are the structural elements of body tissues.

 Proteins are made up of amino acids.

 Proteins give heat and energy to the body and also aid in building and repair.
  Only small amounts of proteins are stored in the body as they can be used up quickly on demand.

 Proteins are considered as the bricks, they make up bones, muscles, hair and other parts of the
body.

 Proteins like enzymes are functional elements that take part in metabolic reactions.

 Antibodies, blood hemoglobin are also made of proteins.

 Proteins have a molecular weight of 5 to 300 kilo-Daltons.

Properties of Proteins

The general properties of proteins are similar to those of the amino acids:

Physical Properties of Proteins

 Proteins are colorless and tasteless.

 They are homogeneous and crystalline.

 Proteins vary in shape; they may be simple crystalloid structure to long fibrilar structures.

 Protein structures are of two distinct patterns - Globular proteins and fibrilar proteins.

 Globular proteins are spherical in shape and occur in plants. Fibrilar proteins are thread-like, they
occur generally in animals.

 In general proteins have large molecular weights ranging between 5 X 103 and 1 X 106.

 Due to the huge size, proteins exhibit many colloidal properties.

 The diffusion rate of proteins is extremely slow.

 Proteins exhibit Tyndall effect.

 Proteins tend to change their properties like denaturation. Many a times the process of
denaturation is followed by coagulation.

 Denaturation may be a result of either physical or chemical agents. The physical agents include,
shaking, freezing, heating etc. Chemical agents are like X-rays, radioactive and ultrasonic
radiations.

 Proteins like the amino acids exhibit amphoteric property i.e., they can act as acids and alkalies.

 As the proteins are amphoteric in nature, they can form salts with both cations and anions based
on the net charge.
  The solubility of proteins depends upon the pH. Lowest solubility is seen at isoelectric point, the
solubility increases with increase in acidity or alkalinity.

 All the proteins show the plane of polarized light to the left, i.e., laevorotatory.

Chemical Properties of Proteins

 Proteins when hydrolyzed by acidic agents, like conc.HCl yield amino acids in the form of their
hydrochlorides.

 Proteins when are hydrolyzed with alkaline agents leads to hydrolysis of certain amino acids like
arginie, cysteine, serine, etc., also the optical activity of the amino acids is lost.

 Proteins with reaction with alcohols give its corresponding esters. This process is known as
esterification.

 Amino acids react with amines to form amides.

 When free amino acids or proteins are said to react with mineral acids like HCl, the acid salts are
formed.

 When amino acid in alkaline medium reacts with many acid chlorides, acylation reaction takes
place.

 Sanger's reaction - Proteins react with FDNB reagent to produce yellow colored derivative, DNB
amino acid.

 Xanthoproteic test - On boiling proteins with conc. HNO3, yellow color develops due to presence
of benzene ring.

 Folin's test - This is a specific test for tyrosine amino acid, where blue color develops with
phosphomolybdotungstic acid in alkaline solution due to presence of phenol group.

Protein Classification

Classification of Proteins Based on Shape

They are grouped under two categories globular and fibrous.

Globular or Corpuscular Proteins

Globular proteins have axial ratio less than 10. They are compactly folded and coiled. and possess a
relatively spherical or ovoid shape. They are usually soluble in water and in aqueous media. Example:
Insulin, plasma albumin, globulin enzymes.

Fibrous or Fibrillar Proteins

These proteins have axial ratio more than 10, hence, they resemble long ribbons or fibres in shape. They
are mostly found in animals, and are not soluble in water or in solution of dilute acids. Fibrous proteins
aid in protection and structural support.
Example: Collagen, Keratin, Elastins, Fibroin.

Classification of Proteins Based on Composition and Solubility

Simple Proteins or Holoproteins

These proteins are made of only one type of amino acid, as structural component, on decomposition with
acids, they liberate constituent amino acids. They are mostly globular type of proteins except for
scleroproteins, which are fibrous in nature.

Simple proteins are further classified based on their solubility.

Protamines and histones - These proteins occur only in animals and are basic proteins. The possess
simple structure and low molecular, are water soluble and are not coagulated by heat. The are strongly
basic in character due to the high content of lysine, arginine. Example: Protamines - salmine, clupine,
cyprinine; Histones - nucleoshistones, globin.

Albumins - They are widely distributed in nature, mostly seen in seeds. They are soluble in water and
dilute solutions of acids, bases and salts. Example: Leucosine, legumeline, serum albumin.

Globulins - They are of two types, pseudoglobulins which are soluble in water, other is euglobulins
which are insoluble in water. They are coagulated by heat. Example: Pseudoglobulin, serum globulin,
glycinine. etc.

Scleroproteins or Albuminoids - These occur mostly in animals and are commonly known as animal
skeleton proteins, they are insoluble in water, and in dilute solution of acids, based and salts.

Conjugated or Complex Proteins or Heteroproteins

These are proteins that are made of amino acids and other organic compounds. The non-amino acid group
is termed as prosthetic group.

Complex proteins are further classified based on the type of prosthetic group present.

Metalloproteins - These are proteins linked with various metals. Example: casein, collagen,
ceruloplasmin, etc.

Chromoproteins - These are proteins that are coupled with a colored pigment. Example: Myoglubin,
hemocyanin, cytochromes, flavoproteins, etc.

Glycoproteins and Mucoproteins - These proteins contain carbohydrates as the prosthetic

group. Example: Glycoproteins - egg albumin, serum globulins, serum albumins; Mucoproteins -
Ovomucoid, mucin etc.

Phosphoproteins - These proteins are linked with phosphoric acid. Example: casein.
Lipoproteins - Proteins forming complexes with lipids are lipoproteins. Example: lipovitellin,
lipoproteins of blood.

Nucleoproteins - These are compounds containing nucleic acids and proteins. Example: Nucleoproteins,
nucleohistones, nuclein.

Derived Proteins

These are proteins that are derived from the action of heat, enzyme or chemical reagents.

Derived proteins are of two types, primarily derived proteins and secondary derived proteins. Primary
derived proteins are derivatives of proteins, in which the size of the protein molecule is not altered
materially, while in secondary derived proteins, hydrolysis occurs, as a result the molecules are smaller
than the original proteins.

Primary derived proteins are classified into three types - Proteans, Infraproteins and Coagulated proteins.
Example: edestan, coagulated eggwhite.

Secondary derived proteins are further classified into 3 types - Proteoses, Peptones and Polypeptides.

Classification of Proteins on Biological Function

Proteins depending upon their physical and chemical structure and location inside the cell, they perform
various functions. Proteins are grouped as follows, based on their metabolic function they perform.

Enzymic Proteins
They are the most varied and highly specialized proteins with catalytic activity. Enzymes catalyze a
variety of reactions. Example: Urease, catalase, cytochrome C, etc.

Structural Proteins
Theses proteins aid in strengthening or protecting biological structures. Example: Collagen, elastin,
keratin, etc.

Transport or Carrier Proteins

These proteins help in transport of ions or molecules in the body. Example: Myoglobin, hemoglobin, etc.

Nutrient and Storage Proteins

These proteins provide nutrition to growing embryos and store ions.

Contractile or Motile Proteins

These proteins function in the contractile system. Example: Actin, myosin, tubulin, etc.

Defense Proteins
These proteins defend against other organisms. Example: Antibodies, Fibrinogen, thrombin.

Regulatory Proteins
They regulate cellular or metabolic activities. Example: Insulin, G proteins, etc.

Toxic Proteins
These proteins hydrolyze or degrade enzymes. Example: snake venom, ricin.
Structure of Proteins

There are four structural levels of organization to describe the complex macromolecule, protein based on
the degree of complexity of of the molecule. They are Primary Structure, Secondary structure, Tertiary
structure and Quaternary structure.

Primary Structure of Protein

 Primary structure of protein is the linear sequence of amino acids that make up the polypeptide
chain.

 his sequence is given by the sequence of nucleotide bases of the DNA in the genetic code.

 The amino acid sequence determines the positioning of the different R groups relative to each
other.

 The positioning determines the way the protein folds and the final structure of the molecule.

Secondary Structure of Protein

 The linear, unfolded structure of polypeptide chain assumes helical shape to produce the
secondary structure.

 The secondary structure refers to the regular folding pattern of twists and kinks of the polypeptide
chain.

 The regular pattern is due to the hydrogen bond formation between atoms of the amino acid
backbone of the polypeptide chain.

 The most common types of the secondary structure are the alpha helix and the ß pleated sheet.

Tertiary Structure of Protein

 Tertiary structure of proteins is the three dimensional structure formed by the bending and
twisting of the polypeptide chain.

 The linear sequence of polypeptide chain is folded into compact globular structure.

 The folding of the polypeptide chain is stabilized by weak, noncovalent interactions.

 These interactions are hydrogen bonds and electrostatic interactions.

 Hydrogen bonds are formed when hydrogen atom is shared with two other atoms.

 Electrostatic interactions between charged amino acid chains.

 Electrostatic interactions are between positive and negative ions of the macromolecules.

 Hydrophobic interactions, disulphide linkages and covalent bonds also contribute to tertiary
structure.
Quaternary Structure of Protein

 Some proteins contain more than one polypeptide chains, this association of polypeptide chains
refers to the quaternary structure.

 Each polypeptide chain is called a subunit.

 The subunits can be same or different ones.

 Example: Haemoglobin the oxygen carrying component of blood is made up of two polypeptide
chains, one with 141 amino acids and the other is a different type of 146 amino acids.

Function of Proteins

Below is the list of proteins functions.

 Proteins are seen in muscles, hair, skin and other tissues; they constitute the bulk of body's non-
skeletal structure. Example: The protein keratin is present in nails and hair.

 Some proteins are hormones and regulate many body functions. Example: Insulin hormone is a
protein and it regulated the blood sugar level.

 Some proteins act enzymes, they catalyze or help in biochemical reactions. Example: Pepsin and
Tripsin.

 Some proteins act as antibodies; they protect the body from the effect of invading species or
substances.

 Proteins transport different substances in blood of different tissues. Example: Hemoglobin is a

oxygen transport protein.

 Contractile proteins help in contraction of muscle and cells of our body. Example: Myosin is
contractile protein.

 Fibrinogen a glycoprotein helps in healing of wounds. It prevents blood loss and inhibits passage
of germs.

Types of Proteins

The types of proteins are as follows:

 Hormones are the proteins based chemicals that are secreted by the endocrine glands. Hormones
are chemical messengers that transmit signals from one cell to the other.

 Enzymatic proteins accelerate the metabolic activity in the cells.

 Structural proteins are necessary components of the body. Structural proteins like collagen forms
connective framework in body tissues, and keratin is main component of hair, skin and nails.

 Defensive proteins like antibodies and immunoglobulin are the core part of the body's immune
system.
  Storage proteins store mainly mineral ions in the body, like potassium, iron etc.

 Transport proteins carry vital materials to the cells.

 Receptor proteins are located on the outer part of the cells, they control the substances that leave
and enter the cell.

 Contractile proteins control the strength and speed of heart and muscle contractions.

Examples of Proteins

Examples of fibrous proteins:

Actin, Collagen, Elastin, Fibronectin, Keratin, Myosin, Tropomyosin, Tubulin, etc

Examples of globular proteins:

Albumins, Alpha globulin, Beta globulin, Cadherin, Fibrin, Gamma globulin, Haemoglobin,
Immunoglobins, Myoglobin, Selectin, Serum albumin, Thrombin etc.

Examples of membrane proteins:

Estrogen receptor, Glucose transporter, Histones, Hydrolases, Oxidoreductases, P53, Rhodopsin, etc.
 What Are the Main Functions of Minerals in the Body?

Minerals are essential nutrients found in many different types of plant- and animal-based foods.
Macro-minerals, or those you require in greater amounts, include calcium, potassium, sodium,
phosphorus, magnesium, chloride, and sulfur. Trace minerals, or those you need in smaller
amounts, include iron, zinc, selenium, manganese, copper, iodine, cobalt, and fluoride. Both
types of minerals support a wide variety of bodily functions, ranging from building and
maintaining healthy bones and teeth to keeping your muscles, heart and brain working properly.

Bone and Tooth Health

Your skeleton provides motility, protection and support for the body. It also stores minerals and
other nutrients. Though they appear hard and unyielding, your bones are actually constantly
being reabsorbed and reformed by your body. Several minerals make up the lattice architecture
of your bones. Calcium is the most abundant mineral in your body and is found in your bones
and blood.

Along with the minerals phosphorus and magnesium, calcium gives your bones strength and
density. This mineral also builds and maintains strong, healthy teeth. Calcium deficiency due to
poor nutrition or illness can lead to osteoporosis, a condition in which the bones become brittle
and less dense, increasing the risk of fractures. KidsHealth notes that foods that are rich in
calcium include milk and other dairy products, green, leafy vegetables and canned fish with
bones.

Energy Production

You require oxygen to produce energy that is necessary for every bodily function and process.
Red blood cells -- or erythrocytes -- carry oxygen to each of your infinite cells, where it is used
to generate energy. Red blood cells contain a heme or iron component that binds to oxygen so
that it can be transported. Without the iron molecules, oxygen could not be attached to the blood
cells and the body would not be able to produce the energy necessary for life. Iron is an essential
mineral, and failing to get enough from your diet can lead to a condition called anemia, which
causes weakness and fatigue. This mineral is primarily found in the blood, and it is also stored in
your liver, spleen, bone marrow and muscles.

Nerve and Muscle Function

Potassium is found in bananas, dates, tomatoes, green leafy vegetables, citrus fruits and legumes
such as peas and lentils. This nutrient is important to keep muscles and the nervous system
functioning normally. Potassium helps to maintain the correct water balance in the cells of your
nerves and muscles. Without this essential mineral, your nerves could not generate an impulse to
signal your body to move, and the muscles in your heart, organs and body would not be able to
contract and flex.
Immune Health

Some minerals such as calcium are needed in large quantities, while others such as zinc are only
needed in trace amounts. Zinc is an essential mineral that is important for keeping your immune
system strong and helps your body fight infections, heal wounds and repair cells. KidsHealth
notes that eating meat and legumes such as beans, peas and lentils will give you sufficient
amounts of zinc. Selenium is also needed in small amounts for immune health. A deficiency of
selenium has been linked to an increased risk of heart disease and even some types of cancers.