STEM 11-3

PROTEINS:
GENERAL BIOLOGY
1
Prepared by: Group 1
 Table of Contents

01 Definition 03 Types of proteins

02 Functions of 04 Structure of
proteins
proteins
 01
ABOUT PROTEINS
INTRODUCTION
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.
About proteins

You need protein in your diet to help your

body repair cells and make new ones.
Protein is also important for growth and
development in children, teens, and
pregnant women.
 PROTEINS
• Proteins are made up of building blocks called amino acids.

• Your body uses them to make new proteins, such as muscle

and bone, and other compounds such as enzymes and
hormones.
 PROTEINS
• It can also use them as an energy source. Some amino acids
can be made by your body – there are 11 of these and
they’re known as non-essential amino acids.

• There are 9 amino acids that your body cannot make, and
they are known as essential amino acids. You need to
include enough of these in your diet so that your body can
function.
 Proteins are made up of hundreds or thousands of
smaller units called amino acids, which are
attached to one another in long chains. There are
20 different types of amino acids that can be
combined to make a protein. The sequence of
amino acids determines each protein’s unique 3-
dimensional structure and its specific function.
Amino acids are coded by combinations of three
DNA building blocks (nucleotides), determined
by the sequence of genes.
Amino acids are classified into three groups:

– Essential
– Nonessential
– Conditional

Essential amino acids cannot be made by the

body, and must be supplied by food. They do not
need to be eaten at every meal. The balance over
the whole day is more important.
Non-essential amino acids are made by the body
from essential amino acids or in the normal
breakdown of proteins.

Conditional amino acids are needed in times of

illness and stress.
02
FUNCTIONS OF
PROTEINS
 Functions of proteins in our body

01 Protein is required for the growth and

maintenance of tissues. Your body’s protein
needs are dependent upon your health and
activity level.

06
02 Enzymes are proteins that allow key chemical reactions
to take place within your body.
 Functions of proteins in our body

03 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.

04 A class of proteins known as fibrous proteins

provide various parts of your body with structure,
strength and elasticity.
 Functions of proteins in our body

05 Proteins in your blood maintain the fluid balance between

your blood and the surrounding tissues.
Proteins form antibodies to protect your body from
foreign invaders, such as disease-causing bacteria and
viruses.

06 Some proteins transport nutrients throughout your

entire body, while others store them.
 Functions of proteins in our body

07 Proteins act as a buffer system, helping your body

maintain proper pH values of the blood and other bodily
fluids.

08 Protein can serve as a valuable energy source but only

in situations of fasting, exhaustive exercise or
inadequate calorie intake.
03
TYPES OF
PROTEINS
There is a total of seven different
protein types under which all proteins
fall. These include antibodies,
contractile proteins, enzymes, hormonal
proteins, structural proteins, storage
proteins, and transport proteins.
 TYPES OF PROTEINS
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.
 TYPES OF PROTEINS
Contractile proteins

Contractile proteins are responsible for muscle contraction and

movement, see Molecular Motors).

The cytoplasm of cells is a colloidal network of contractile

proteins. Actin filaments are the major components of this
network. See Muscle Cells (Myocyte)
Eukaryotes tend to possess copious amounts of actin, which
controls muscle contraction as well as cellular movement and
division processes. Myosin powers the tasks carried out by
actin by supplying it with energy.
 TYPES OF PROTEINS
Enzymes

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.
 TYPES OF PROTEINS
Hormonal proteins

Hormonal Proteins: Hormonal proteins are messenger proteins

that help coordinate certain bodily functions.

Growth factors are highly specific proteins, a subdivision of

cytokines. Growth factors stimulate the division and
differentiation of a particular type of cell. In skeletal muscle
hypertrophy, growth factors include insulin-like growth factor
(IGF). IGF is secreted by skeletal muscle. It regulates insulin
metabolism and stimulates protein synthesis.
 Hormonal proteins

Testosterone is an androgen, or a male sex hormone. The

primary physiological role of androgens are to promote the
growth and development of male organs and characteristics.
Testosterone affects the nervous system, skeletal muscle, bone
marrow, skin, hair and the sex organs.

Cortisol is a steroid hormone (hormones which have a steroid

nucleus that can pass through a cell membrane without a
receptor) which is produced in the adrenal cortex of the kidney.
It is a stress hormone.
 TYPES OF PROTEINS
Structural proteins

A large group of structural proteins maintains and

protects the structure of the animal body.
The most common example of a structural protein is
collagen which is found in the bones, cells and skin.
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.
 TYPES OF PROTEINS
Storage proteins

Storage proteins reserve amino acids for the body

until ready for use. Examples of storage proteins
include

Ferritin a storage protein that stores iron regulates

insulin metabolism and stimulates protein synthesis.
 TYPES OF PROTEINS
Transport proteins

Transport proteins are carrier proteins that move

molecules from one place to another in the body.

The respiratory protein hemoglobin acts as oxygen

carrier in the blood, transporting oxygen from the lung to
body organs and tissues.
Cytochromes, another type of transport protein, operate
in the electron transport chain as electron carrier
proteins.
04
PROTEIN
STRUCTURE
 STRUCTURE OF PROTEINS
Biochemists have distinguished several levels of structural
organization of proteins.

They are:
– Primary structure
– Secondary structure
– Tertiary structure
– Quaternary structure
 PRIMARY STRUCTURE
• The primary structure of protein
refers to the sequence of amino acids
present in the polypeptide chain.
• Amino acids are covalently linked
by peptide bonds.
• Each component amino acid in a
polypeptide is called a “residue” or
“moiety”
• By convention, the 10 structure of a
protein starts from the amino-
terminal (N) end and ends in the
carboxyl-terminal (C) end.
 IMPORTANCE OF PRIMARY STRUCTURE
1. To predict 20 and 30 structures from sequence
homologies with related proteins. (Structure prediction)
2. Many genetic diseases result from abnormal amino
acid sequences.
3. To understand the molecular mechanism of action of
proteins.
4. To trace evolutionary paths.
 SECONDARY STRUCTURE
• Spatial folding of the polypeptide chain in properly arranged,
repetitive structures.

Three types of secondary structures:

α-helix
β-sheet
β-turn.
 Alpha (a) helix
The carbonyl oxygen of each peptide bond
is linked to a hydrogen bond with the amide
hydrogen of the fourth amino acid towards
the C-terminus.

Formed as a result of hydrogen bonds

between the carbonyl oxygen (C = O) and
the amide hydrogen (N-H) of the
polypeptide chain and does not depend on
the side radicals.
 Features of Alpha helix

• Most common and stable conformation.

• Spiral structure: Polypeptide bonds form the backbone of the spiral.

R-groups of the amino acids remain outwards of the spiral.

• Stabilized by H-bonds: Hydrogen bonds are week but collectively

determine the stability of α-helix.
 Beta (b) – pleated sheet
Parallel – run in the same
direction with longer looping
sections between them

Anti-parallel beta sheets:

polypeptide chains run in an
opposite direction
Both models are found in proteins, but the antiparallel structure is more stable than the
parallel beta-sheet.
 B - turn
Permits the change of direction of the peptide chain to get a folded
structure.

Beta-turn loops allow for protein compaction, since the hydrophobic

amino acids tend to be in the interior of the protein, while the
hydrophilic residues interact with the aqueous environment.
 TERTIARY STRUCTURE

Complete three-dimensional shape of a given

protein. Conformation.

Represent the spatial relationship of the

different secondary structures to one
another within a polypeptide chain and how
these secondary structures themselves fold
into the three-dimensional form of the The spiral regions represent sections of the
protein. polypeptide chain that have an α-helical structure,
while the broad arrows represent β-pleated sheet
structures.
 Tertiary structure: describes the relationship of different domains to
one another within a protein.
• A domain is a basic structural unit within a
protein molecule.
• Part of protein that can fold into a stable
structure independently.
• Different domains can possess different
functions.
• Proteins can have one to many domains
depending on protein size.
Pyruvate kinase (a monomeric
• A polypeptide with 200 amino acids consists of protein): three domains
two or more domains.
Tertiary structure is based on various types of interactions between the
side-chains of the peptide chain.
Stabilizing Interactions of Tertiary Structures
 GLOBULAR PROTEINS
Globular proteins fold up into compact, spherical shapes.

Their functions are related to cell metabolism: biosynthesis and

biodegradation, transport, catalytic function.

Hydrophobic R-groups are oriented into inner part of the protein

molecule, while hydrophilic R-groups are pointed towards molecule
edges.

• Globular proteins are water soluble.

 GLOBULAR PROTEINS
Example: myoglobin

Globular protein that stores oxygen in

muscles

A single peptide chain that is mostly a-

helix

O2 binding pocket is formed by a heme

group and specific amino acid side-
 FIBROUS PROTEINS

Much or most of the polypeptide chain is parallel to a single axis

Fibrous proteins are often mechanically strong and highly cross-linked

Fibrous proteins are usually insoluble

• Usually play a structural role

For example, a-keratins are fibrous proteins that make hair, fur, nails and
skin
- hair is made of twined fibrils
• - the a-helices are held together by disulfide bonds
 FIBROIN PROTEINS
Fibroins are the silk proteins. They also form the spider webs
Made with a b-sheet structures with Gly on one face and Ala/Ser on the other
Fibroins contain repeats of [Gly-Ala-Gly-Ala-Gly-Ser-Gly-Ala-Ala-Gly-(Ser-Gly-
Ala-Gly-Ala-Gly)8]
The b-sheet structures stack on top of each other
Bulky regions with valine and tyrosine interrupt the b-sheet and allow the
stretchiness
 QUATERNARY STRUCTURE

Monomeric proteins:

– built of a single polypeptide chain.

Oligomeric proteins:

– built of more than one polypeptide chains called subunits or

monomers.
 QUARTERNARY STRUCTURE
Quaternary structure describes the joining of two or more polypeptide
subunits.

The subunits each have their own tertiary structure.

Bonds – non-covalent interactions.

Subunits can either function independently or work co-operatively.

For example: Hemoglobin

A globular protein that consists of four subunits (2α and 2β, of two different types (α and β)
Each subunit contains a heme group for O2 binding
Binding O2 to one heme facilitates O2 binding by other subunits
Replacement of even one amino acid in primary structure with another amino acid is critical
for the function of the protein.
STRUCTURAL ORGANIZATION OF PROTEINS: SUMMARIZE
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