2. PROTEIN
Are the most abundant organic
compounds found in any living
organism.
They are necessary for the structure,
function, and regulation of the
body's tissues and organs and are
vital to the majority of the work
performed by cells.
6. are generally the standard parts
of an amino acid
THE PRIMARY STRUCTURE OF A PROTEIN CONTAINS:
are also part of the amino acid but
may vary in different ways such as;
hydrophilic – water loving and
hydrophobic – resistant to water
These are the building blocks proteins
that is held by a peptide bond
R GROUPS
AMINO ACIDS 2
3
1 AMINO GROUPS AND
CARBOXYL GROUPS
4 POLYPEPTIDE CHAINS
are a sequence of amino acids
joined together by covalent or
peptide bonds.
7. PRIMARY
STRUCTURE
The attachment that occurs in the
Primary Structure of protein is done
during the process of protein
biosynthesis or translation.
Genes, that makes up the DNA
determines the order or sequence and
how many amino acids are there in
polypeptide chain
8. SECONDARY STRUCTURE
On this stage, folding is much more
emphasized as the chains may fold into
different ways such as:
secondary
structure Alpha Helix (a-helix)
1.
Beta-pleated Sheet (β-pleated sheet)
2.
9. ALPHA HELIX (A-
HELIX) AND BETA-
PLEATED SHEET
(Β-PLEATED
SHEET)
These two folding structures
are defined by hydrogen bonds
between the main chain and
peptide groups – these
hydrogen bonds are involved
in the backbone of the amino
acid structure
10. TERTIARY STRUCTURE
The folds on this stage is much more defined
in a 3D shape of a functional protein
The folds in this stage are mainly caused by
the R groups(side chains) because
hydrophilic R groups hang on the outside
while hydrophobic R groups are on the
inside part of the protein forming the 3D
shape of the protein
tertiary
structure
11. OTHER R GROUP INTERACTIONS:
Ionic Bonds
Hydrogen bonds
Disulfide bonds (disulfide
bridges)
Van Der Waals
interactions
12. At this stage, the protein consist of more
than one polypeptide chain where each
chain may be a subunit
Examples of proteins like this is the oxygen-
transporting molecule hemoglobin which
has four subunits and another example is
collagen fibers
QUATERNARY STRUCTURE
quaternary
structure
14. STRUCTURAL
PROTEIN
1.
They are found in the hair of mammals
Are proteins that living organisms use to
maintain their shape or structural
integrity.
Some common structural proteins are
keratin and collagen.
The shape of proteins determines the
protein's function and there are
generally two shapes of proteins which
are globular and fibrous
EXAMPLES OF
STRUCTURAL PROTEIN
GLOBULAR
FIBROUS
15. GLOBULAR FIBROUS
can sometimes be referred to
as spheroproteins due to its
spherical shape
are usually more sensitive to
heat
are generally soluble in water
have an irregular amino acid
sequence
usually act as Enzymes that
speed up chemical reactions.
are narrower and more
prolonged and can also be
referred to as scleroproteins
are usually less sensitive to heat
are generally not soluble in
water
have a regular amino acid
sequence
often play a structural role in
nature.
16. 2. CONTRACTILE
PROTEIN
Proteins that provide muscular
movement to be specific, it aids in the
contraction of muscles.
The contractile proteins actin and
myosin are the most crucial.
Both actin and myosin function by
controlling the voluntary muscular
movements within the body
EXAMPLES OF
CONTRACTILE PROTEIN
ACTIN
MYOSIN
17. ACTIN MYOSIN
produces thin and short
contractile filaments within
muscle cells.
Actin filaments have a smooth
surface.
produces dense/thick and long
contractile filaments within
muscle cells.
myosin filaments have a rough
surface.
18. 3. STORAGE
PROTEINS
protein that acts as a reservoir of metal
ions and amino acids, which can be
combined and used for maintenance
and growth
a type of protein that is stored inside
cells or tissues as food and can be
assembled when needed to provide
energy.
This type of protein stores amino acids
for the body until it is ready for use.
19. ANIMAL STORAGE
PROTEIN
Ovalbumin - found in the
white part of an egg.
Casein - found in large
amounts in mammalian
milk.
Ferritin - found in liver,
chicken, tofu, lentils, and
beans
Seed storage protein - stored at
high levels in the seed at the last
stage of seed development.
-- these are the primary proteins of
all types of grains.
Vegetative storage protein -
proteins that collect in plant
tissues such as leaves, stems, etc -
found in soybean, potato, sweet
potato, etc
TYPES OF STORAGE PROTEINS
PLANT STORAGE
PROTEIN
20. 4. DEFENSIVE PROTEIN
Defensive proteins or antibodies are produced by the
body to fight diseases and prevent injury.
also referred to as immunoglobulins are the central
most important part of the entire immune system.
These proteins help in keeping disease at par by
maintaining several forms of barriers and elimination
mechanisms for the body
Examples of defense proteins include antibodies,
lectins, and antiviral proteins.
21. 5. TRANSPORT PROTEIN
serves the function of moving other materials within
an organism
Example/s: Carrier proteins
22. 6. SIGNAL PROTEIN
play a vital role in functioning of the brain
controls a wide array of cellular functions, including
motility, hormone responses, sensory perception, and
neurotransmission.
Hormones that help coordinate body activities
Proteins that transmit signals to coordinate biological
processes between different cells, tissues, and organs
Example/s: Growth hormone
23. 7. ENZYME
proteins that act as biological catalysts by accelerating
chemical reactions.
These are biomolecules that speed up the chemical
reaction in the cells
Vital in life processes like digestion and metabolism
25. OTHER PROTEINS :
INTEGRAL PERIPHERAL
Are proteins that are
embedded within the
phospholipid bilayer
and is present in both
active and passive
transport
Are proteins that are
associated with the
membrane but is not
embedded to the
phospholipid bilayer
unlike integral proteins
