PROTEINS

ITS FUNCTIONS AND TYPES

Reported by: Group 3

 What is Proteins?
Proteins are large, complex molecules that play many
critical roles in the body. They do most of the work in
cells and are required for the structure, function, and
regulation of the body’s tissues and organs.

Proteins are made up of hundreds or thousands of

smaller units called amino acids, which are attached to
one another in long chains.
 First described by the Dutch chemist Gerardus
Johannes Mulder, protein got its name from Swedish
chemist Jöns Jacob Berzelius in 1838. The name
"protein" is derived from the Greek word for
"primary," meaning "in the lead"or "standing in
front." Early scientists believed that protein was an
essential nutrient for maintaining the body's overall
structure, and its importance has been studied for
centuries.
 TION OF
NC P
U

RO
F
Your body uses protein to
MAIN

TEI
develop and repair its tissues. It
powers metabolic processes,

N
maintains fluid and pH a state of
balance and strengthens the
immune system. In addition, it can
serve as an energy source and
transport and store nutrients.
Types of Protein
 ANTIBODIES
are specialized proteins that defend the body against antigens or foreign
invaders. Their ability to travel through the bloodstream enables them to be
utilized by the immune system to identify and defend against bacteria,
viruses, and other foreign intruders in blood. One way antibodies counteract
antigens is by immobilizing them so that they can be destroyed by white
blood cells.
Example:
OF ANTIBODIES

IgG, the most common antibody, is present

mostly in the blood and tissue fluids, while IgA
is found in the mucous membranes lining the
respiratory and gastrointestinal tracts
 Contractile Proteins

Contractile proteins are responsible for muscle contraction and movement.

Contractile proteins are proteins that mediate sliding of contractile fibres
(contraction) of a cell's cytoskeleton, and of cardiac and skeletal muscle.

The contractile proteins are myosin, the principal component of thick myofilaments,
and actin, which is the principal component of thin myofilaments.
 Enzymes
Enzymes are proteins that help speed up metabolism, or the chemical reactions in
our bodies. They build some substances and break others down. All living things
have enzymes. Our bodies naturally produce enzymes. But enzymes are also in
manufactured products and food. They are essential for respiration, digesting
food, muscle and nerve function, among thousands of other roles. Each cell in the
human body contains thousands of enzymes. Enzymes provide help with facilitating
chemical reactions within each cell.
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.
Example:
Lipase is an enzyme the body uses to break
down fats in food so they can be absorbed
in the intestines. Lipase is produced in the
pancreas, mouth, and stomach.

02
Hormonal Proteins
Hormonal proteins are messenger proteins that help coordinate certain
bodily functions.
Some proteins function as chemical-signaling molecules called hormones. These
proteins are secreted by endocrine cells that act to control or regulate specific
physiological processes, which include growth, development, metabolism, and
reproduction.

FOR EXAMPLE, INSULIN IS A PROTEIN HORMONE THAT HELPS TO REGULATE BLOOD

GLUCOSE LEVELS. OTHER PROTEINS ACT AS RECEPTORS TO DETECT THE
CONCENTRATIONS OF CHEMICALS AND SEND SIGNALS TO RESPOND.
STRUCTURAL PROTEINS
Structural proteins are a category of proteins responsible for functions
ranging from cell shape and movement to providing support to major
structures such as bones, cartilage, hair, and muscles. This group includes
proteins such as collagen, actin, myosin, and keratin.
A large group of structural proteins maintains and protects the structure of the animal bod
Structural proteins are also found in cells. They are used to provide an internal structure to the cell (the
cytoskeleton) and are sometimes involved in cell movement. Structural proteins are especially important in
larger cells.
EXAMPLES:
The most common example of a structural protein is collagen which is found in the bones, cells and skin.
Structural proteins such as collagen, fibronectin and laminin are utilized in cell culture applications as
attachment factors.
 Storage Proteins
Storage proteins accumulate in both vegetative and reproductive tissues and
serve as a reservoir to be used in later stages of plant development. The
accumulation of storage protein is thus beneficial for the survival of plants.
Storage proteins are also an important source of dietary plant proteins. One
of the main characteristics of storage proteins is that they accumulate in
high levels in specific tissues at a specific stage of development.
 Example:
Ferritin is a protein that stores iron. Red
blood cells need iron to form normally
and carry oxygen around your body.
Other parts of your body, such as your
liver, bone marrow, and muscles, also need
iron.
Transport Proteins
Transport proteins are carrier proteins that move molecules from one
place to another in the body. Transport proteins act as doors to the
cell, helping certain molecules pass back and forth across the plasma
membrane, which surrounds every living cell. In passive transport
molecules move from an area of high concentration to an area of low
concentration.
 Example:
Haemoglobin protein is a transport protein or carrier
protein because it carries oxygen from lungs to the other
part of the human body.
Levels of Protein Structures
Proteins fold into stable three‐dimensional shapes,
or conformations, that are determined by their
amino acid sequence. The complete structure of a
protein can be described at four different levels of
complexity
Primary Structure
Secondary Structure
Tertiary Structure
Quaternary structure
 Primary Structure
The simplest level of protein structure, primary structure, is simply the sequence of amino acids in a
polypeptide chain. Linear amino acid sequence of a protein's polypeptide chain .The protein ‘s primary
structure is the amino acid sequence in its polypeptide chain. If proteins were popcorn stringers designed
to decorate a Christmas tree, a protein ‘s primary structure is the sequence in which various shapes and
varieties of popped maize are strung together.

Definition:
Polypeptide chain-is a string of amino acids connected together by peptide bonds. The word poly means many, and the word peptide refers to
proteins. So, a polypeptide chain is a chain of the building blocks of proteins or amino acids.
 Secondary
Structure
Secondary structure is defined as the local spatial conformation of
the polypeptide backbone excluding the side chains. The proteins do
not exist in just simple chains of polypeptides.
These polypeptide chains usually fold due to the interaction between
the amine and carboxyl group of the peptide link.
The structure refers to the shape in which a long polypeptide chain
can exist. The most common types of secondary structures are the
α helix and the β pleated sheet. Both structures are held in shape
by hydrogen bonds, which form between the carbonyl O of one
amino acid and the amino H of another.
Tertiary structure
The tertiary structure of a protein molecule
encompasses the overall folding of polypeptide
chains, where, if more than one chain is present, the
chains are linked by covalent bonds—most often
disulfide bonds .The overall three-dimensional
structure of a polypeptide is called its tertiary
structure. It gives rise to two major molecular
shapes called fibrous and globular.
 Quaternary structure
The quaternary structure of a protein refers to the
arrangement of multiple protein subunits in a single
protein complex. Many proteins are made up of a single
polypeptide chain and have only three levels of
structure (the ones we’ve just discussed). However,
some proteins are made up of multiple polypeptide
chains, also known as subunits. When these subunits
come together, they give the protein its quaternary
structure. Each of the subunits has its own primary,
secondary, and tertiary structure. The subunits are
held together by hydrogen bonds and van der Waals
forces between nonpolar side chains.
Levels of
Protein
Structure
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