What are proteins?

Proteins are polymers. A protein is made from one or more polypeptide chains, where each
polypeptide chain is built from smaller molecules called “amino acids”.

Topic: Classification of proteins by composition (simple,

complex) and by function. Composition and levels of structural
organization of proteins.
Learning objectives:11.4.1.3 classify proteins by their
structure, composition and functions;
11.4.1.4 describe the four stages of protein organization and
explain the types of links at each level of protein structure
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

Criterion Students should know:

 be able to classify  Features of the

proteins according to classification of proteins
according to their
their structure,
structure, composition
composition and and functions.
functions;  Names the main four
 describe the four stages stages of protein
of protein organization organization and
and explain the types of explains the types of
bonds at each level of
links at each level of
the protein structure.
protein structure
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

Terms
 Рrotein  Hydrolysis
 Amino acids  Condensation
 Сovalent bond  Amino group
 Peptide bond  Carboxyl group
 Ionic bond  Polypeptides
 Disulfide bond  Primary structure
 Hydrogen bond  Secondary structure
 Hydrophobic
 Tertiary structure
interactions  Quaternary structure
 Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure
Classify Proteins by their Structure, Composition and Function
Proteins are classified based on the following three criterion:
1.Classification based on Structure of Protein.
2.Classification based on Composition of Protein.
3.Classification based on Functions of Proteins.
They have a linear shape (secondary structure).
Physically fibrous proteins are very tough and strong.
They are insoluble in water. Functions of fibrous proteins:
perform structural functions in cells. Examples of fibrous
proteins: Collagen, Myosin, Silk, Keratin.
Globular proteins have a globular shape (tertiary structure).
Physically, they are softer than fibrous proteins. They dissolve
easily in water. Most proteins in cells are globular proteins.
Functions: form enzymes, antibodies and some hormones.
Example: insulin, hemoglobin, DNA polymerase, RNA
polymerase.

Their structure is intermediate in relation to linear and globular

structures. These are short proteins with a more or less linear
shape. Unlike fibrous proteins, they are water soluble.
Function: blood clotting proteins.
Example: Fibrinogen.
 Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

Conjugated proteins.
•They contain one or more non-amino acid
components. Here the protein part is tightly or
loosely bound to one or more non-proteins parts.
The non-protein parts of these proteins are called
prosthetic groups. The prosthetic group may be
metal ions, carbohydrates, lipids, phosphoric acids,
nucleic acids and FAD. The prosthetic group are
essential for the biological functions of these
proteins. Conjugated proteins are usually globular
in shape and are soluble in water. Most of the
enzymes are conjugated proteins. Based on the
nature of prosthetic groups, the conjugated
proteins are further classified as follows:
•Phosphoprotein: prosthetic group is phosphoric
acid, example – Casein of milk, Vitellin of egg yolk.
•Glycoproteins: Prosthetic group is carbohydrates,
Example – Most of the membrane proteins, Mucin
(component of saliva).
•Nucleoprotein: Prosthetic group is nucleic acid,
Example – proteins in chromosomes, structural
proteins of ribosomes.
•Chromoproteins: Prosthetic groups is pigment or
Simple Proteins. chrome, Example : heamoglobin, Phytochrome,
 Simple proteins composed of ONLY amino Cytochrome.
acids. •Lipoproteins: Prosthetic group is Lipids, Example:
 Proteins may be fibrous or globular. Membrane Proteins.
•Flavoproteins: Prosthetic group is FAD (Flavin
 They possess relatively simple structural Adenine Dinucleotide), Example: Proteins of
organization. Electron Transport System (ETS).
 Example: Collagen, Myosin, Insulin, •Metalloproteins: Prosthetic group is Metal ions,
Keratin. Example: Nitrate Reductase.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

What are the main functions of proteins?

 Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

Proteins have many important

functions
 all enzymes are proteins (DNA Polymerase, Nitrogenase, Lipase.)
 proteins are essential components of cell membranes – their functions in
membranes, such as receptor proteins and signalling proteins
 some hormones are proteins – for example, insulin and glucagon
 the oxygen-carrying pigments haemoglobin and myoglobin are proteins
 antibodies, which attack and destroy invading microorganisms, are
proteins
 collagen, another protein, adds strength to many animal tissues, such as
bone and the walls of arteries
 hair, nails and the surface layers of skin contain the protein keratin
 actin and myosin are the proteins responsible for muscle contraction
 proteins may be storage products – for example, Ferritin which stores
iron, casein, Gluten of wheat, in milk and ovalbumin in egg white
 They are toxic proteins. Example: Snake venom.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
types of links at each level of protein structure

Activity
Match the pictures with the functions of the protein
 Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and
explain the types of links at each level of protein structure

What is the difference between these drawings?

There are a total of 20 amino acids that can be arranged in trillions upon trillions of different
ways to create proteins that serve a huge variety of functions. Amino acids can link together in a
huge variety of ways to create different proteins. 
A polypeptide is a chain of amino acids and is the simplest form of a protein. Amino acids bond
together by peptide bond to form long, linear chains that can be more than 2000 amino acids
long. 
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

What are the main groups (components) that make up the amino
acid?
The general structure of an amino acid.

The general structure of all

amino acids and of glycine, the
simplest amino acid. They all
have a central carbon atom
which is bonded to an amine
group, –NH2, and a carboxylic
acid group, –COOH. It is these
two groups which give amino
acids their name. The third
component that is always
bonded to the carbon atom is a
hydrogen atom.

b Structure of the simplest amino acid, glycine, in which

the R group is H, hydrogen. R groups for the 20 naturally
occurring amino acids
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

Fill in the missing words in the text below using keywords

Keywords: condensation, uniquely, carboxyl group, covalent,
hydrolysis, amine group, stable, water,
 Amino acids are bonded together between the amine group (-NH₂) of one amino acid and
the carboxyl group (-COOH) of a second amino acid. As two amino acids bond together,
one hydrogen ion is removed from the amine group and a hydroxyl group is removed from
the carboxyl group.  The amine group and carboxyl group bond together and a water
molecule is produced as a by product. The bond is known as a ‘peptide bond’. These are
examples of covalent chemical bonds, and are stable. When two amino acids are joined,
the reaction releases a molecule of water. This is type of reaction is called
a condensation reaction. Hydrolysis is the reverse of the condensation reaction, involving
breaking the peptide bond using a molecule of water.
 The R groups of the 20 amino acids each have their own unique structure and chemical
properties. The structure and chemical properties (such as reactivity and boiling
temperature) of a polypeptide and ultimately a protein is determined by the unique
sequence of R groups that extend from the polypeptide backbone. As R groups are attracted
or repelled from each other, the polypeptide chain bends and twists into a uniquely shaped
protein.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

What is dipeptide and polypeptide?

The new molecule which has been formed, made up of two linked
amino acids, is called a dipeptide. A molecule made up of many amino
acids linked together by peptide bonds is called a polypeptide.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the
Primary – The
primary structure of a
protein is the linear
polypeptide chain
formed by the amino
acids in a particular
sequence. Changing
the position of even a
single amino acid will
result in a different
chain and hence a
different protein.
types of links at each level of protein structure
Four stages of protein organization
Secondary – The secondary Tertiary – The tertiary Quaternary – This
structure of a protein is formed by structure is the final 3- structure is
hydrogen bonding in the polypeptide dimensional shape exhibited only by
chain. These bonds cause the chain acquired by the those proteins
to fold and coil in two different
polypeptide chains which have
conformations known as the α-helix
under the attractive and multiple
or β-pleated sheets. The α-helix is
repulsive forces of the polypeptide chains
like a single spiral and is formed by
hydrogen bonding between every different R-groups of combined to form
fourth amino acid. The β-pleated each amino acid. This a large complex.
sheet is formed by hydrogen is a coiled structure that The individual
bonding between two or more is very necessary for chains are then
adjacent polypeptide chains. protein functions. called subunits.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links
at each level of protein structure

Fill in the gaps in

the table
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links
at each level of protein structure

Similarities Between Difference Between Primary Secondary and

Primary Secondary Tertiary Structure of Protein
Tertiary Structure of
Protein
 Primary, secondary, and Definition
tertiary structure are Primary structure of a protein is the linear sequence of
three, structural amino acids, the secondary structure of a protein is the
folding of the peptide chain into an α-helix or β-sheet while
arrangements of
the tertiary structure is the three-dimensional structure of a
proteins. protein. This explains the basic difference between primary
 The basic unit of all of secondary and tertiary structure of protein.
the structures is the
Shape
amino acid As said in the definition, the primary structure of a protein
sequence, which is the is linear, the secondary structure of a protein can be either
primary structure of an α-helix or β-sheet while the tertiary structure of a protein
protein. is globular. 
 Secondary structure of Bonds
protein is formed from Primary structure of a protein is composed of peptide
its primary structure, bonds formed between amino acids, secondary structure of
which in turns form the a protein encompasses hydrogen bonds while the tertiary
tertiary structure. structure of a protein encompasses disulfide bridges, salt
 Each type of structure
https://pediaa.com/difference-between-primary-se
bridges, and hydrogen bonds. This is a main
condary-and-tertiary-structure-of-protein/
has a unique role in the difference between primary secondary and tertiary
structure of protein.
cell.
 Conclusion

 Primary structure of protein is the amino acid sequence, which

is linear. It is produced during translation.
 Secondary structure of protein is either an α-helix or β-sheet
formed due to the formation of hydrogen bonds. It plays a
major role in the formation of structures such as collagen,
elastin, actin, myosin, and keratin fibers.
 Tertiary structure of protein is globular and it is formed due to
the formation of disulfide and salt bridges. It plays a vital role
in  metabolism.
 The difference between primary secondary and tertiary
structure of protein is their structure, bonds, and the role in the
cell.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

A variety of chemical interactions determine the proteins' tertiary

structure. These include hydrophobic interactions, ionic bonding,
hydrogen bonding, and disulfide linkages.

Identify these types of chemical bonds in the picture.

 Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

Key Takeaways: Proteins

 Proteins are long chains of amino acids which fold into precise shapes. Biuret reagent can be
used to test for proteins. The linkages that join amino acids are called peptide bonds. The
sequence of amino acids in a protein, known as its primary structure, determines the way that
it folds and hence determines its three dimensional shape and function.
 Many proteins contain areas where the amino acid chain is twisted into an α-helix; this is an
example of secondary structure. The structure forms as a result of hydrogen bonding between
the amino acids. Another secondary structure formed by hydrogen bonding is the β-pleated
sheet. Further folding of proteins produces the tertiary structure. Often, a protein is made from
more than one polypeptide chain. The association between the different chains is the
quaternary structure of the protein. Tertiary and quaternary structures are very precise and are
held in place by hydrogen bonds, disulfide bonds (which are covalent), ionic bonds and
hydrophobic interactions.
 Proteins may be globular or fibrous. A molecule of a globular protein – for example
haemoglobin – is roughly spherical. Most globular proteins are soluble and metabolically
active. Haemoglobin contains a non-protein (prosthetic) group, the haem group, which
contains iron. This combines with oxygen. A molecule of a fibrous protein – for example,
collagen – is less folded and forms long strands. Fibrous proteins are insoluble. They often
have a structural role. Collagen has hightensile strength and is the most common animal
protein, being found in a wide range of tissues.
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

Let's do some Reflection 

 What goal did we study today?
 What terms do you remember?

 How can proteins be classified according to their

structure, composition and function?

 Describe the four stages of protein organization and

explain the types of bonds at each level of protein

structure?
 Additional materials
 Protein Structure and Folding
https://www.youtube.com/watch?v=hok2hyED9go&ab_channel=AmoebaSisters
 PROTEIN FOLDING
https://www.youtube.com/watch?v=1peFJ_-N7V8&ab_channel=NeuralAcademy
 Protein Shape - Levels Of Protein Structure - Shape Of Proteins - What Is
Protein Denaturation
https://www.youtube.com/watch?v=YhTpnRzp-eQ&ab_channel=WhatsUpDude
 Protein Structure - Primary - Secondary - Tertiary - Quaternary - Structure of
Protein
https://www.youtube.com/watch?v=ki9dwhCwMsI&ab_channel=5MinuteSchool
Objective: classify proteins by their structure, composition and functions and describe the four stages of protein organization and explain the types of links at each level of protein structure

What is Difference Between the Alpha Helix and Beta Sheet Secondary
Structure of Proteins? 
The most common types of secondary
structures are the α helix and the β pleated
sheet. In an α - helix, the carbonyl (C=O) of
one amino acid is hydrogen bonded to the
amino H (N-H) of an amino acid that is four
down the chain. (E.g., the carbonyl of amino
acid 1 would form a hydrogen bond to the N-H
of amino acid 5). This pattern of bonding pulls
the polypeptide chain into a helical structure
that resembles a curled ribbon, with each turn
of the helix containing 3.6 amino acids. The R
groups of the amino acids stick outward from
the α - helix, where they are free to interact.
In a β - pleated sheet, two or more segments
of a polypeptide chain line up next to each
other, forming a sheet-like structure held
together by hydrogen bonds. The hydrogen
bonds form between carbonyl and amino groups
The α-helix and β-pleated sheet of backbone, while the R groups extend above
and below the plane of the sheet. The strands
of a β - pleated sheet may be parallel, pointing
in the same direction (meaning that their N-
and C-termini match up), or antiparallel,
pointing in opposite directions (meaning that
the N-terminus of one strand is positioned next
to the C-terminus of the other).
Mind MAP Proteins