Protein can be described as :

1. Primary structure
2.Secondary structure
3.Tertiary structure
4.Quaternary structure
The primary structure of protein is the
sequence of amino acid that make up the
polypeptide chain by peptide bond.
Two amino acid join in a condensation
reaction to form a dipeptide. These process
can be repeated to form polypeptide chain
which may contain thousand of amino acid.
A protein is made up of one or more of these
polypeptide chain.
The secondary structure of a protein is the
arrangement of the polypeptide chain into a
regular, repeating three-dimensional
structure held together by hydrogen bond.
Interaction between the amino acid in the
polypeptide chain cause the chain to twist
and fold into a three dimensional shape.
Length of the chain may first coil into alpha
helix or come together in beta pleated sheet.
These are known as secondary structure.
Alpha helix, a spiral coil with the
peptidic bonds forming the backbone
and the R groups per trading in all
directions. Another is the beta pleated
sheet in which the polypeptide chain
fold into regular pleats held together by
hydrogen bonds between the amino
acid and carboxyl ends of the amino
acids.
Most fibrous protein have these type of
structure.
A poly peptide chain often bent and fold to
produce a pre-sized three dimensional shape
which are held by hydrogen bond, sulfur
bridge bond and ionic bond between the
amino acid. The folding of the poly peptide
coil is known as tertiary structure.
Chemical bond and hydrophobic interaction
between R group maintain this tertiary
structure of the protein. Example; myoglobin
has tertiary structure.
The three dimensional arrangement of more
than one tertiary poly peptide coil is called
quaternary structure.
Only protein with several poly peptide chain
have a quaternary structure and single chain
protein have a tertiary structure.
Example; insulin, haemoglobin, glucagon,
lysosome has quaternary structure.
Pg 18, 1st 3 para & fig D
Type of Protein

1) Fibrous Protein
2) Globular Protein
3) Conjugated Protein
 Fibrous Protein
 Fibrous protein have secondary structure.
 They are long, parallel, polypeptide chain with
occasional cross linkage that form them into
fibre.
 They are insoluble in water and are very tough.
Fibrous protein appear in the structure of
connective tissue in tendons and the matrix of
bone and as the keratin that makes up hair ,
nails, horns and feathers .
Example of fibrous protein
Collagen. Pg: 18 last para
 Globular Protein
 Globular protein have complex tertiary and sometimes
quaternary structure.
 Physically they are not tough and soluble in water
 The character of the R group on the amino acid plays
an important role in the formation of globular protein.
 Some R groups are hydrophobic. They repel water and
will not mix or dissolve it. They are usually found on
the inside of globular protein. Some R groups are
hydrophilic-they have an affinity for water. These
groups tend to be found on the outside of globular
protein. The large size of these globular protein
molecules affects their behavior in water.
Pg: 19 2nd para under the headline
Pg: 19, last para, Fig: E
 Conjugated Protein
The shape of a protein molecule is usually very
important in its function. Some protein molecules are
joined with another molecule called a prosthetic group.
These structural feature usually affects the
performance and function conjugated protein-
Haemoglobin is a large protein with iron as the
prosthetic group. It is a conjugated protein as well
globular protein.
 Lipoprotein are formed when proteins are conjugated
with lipids. Lipoprotein are very important in the
transport of cholesterol in the blood.
Glycoprotein are protein with a carbohydrate prosthetic
group. The carbohydrate part of the molecule helps
them to hold a lot of water and also makes it harder for
protein digesting enzymes to break them down.
Water
 Two atom of hydrogen are joined to one atom of oxygen to make up each
water molecule. Each water molecule is slightly polarized. This means it
has a very slightly negative charge - The oxygen atom and very slightly
positive charge - The hydrogen atom. This separation of charge is called a
dipole and the tiny changes are represented as δ+ and δ- .
 The slightly negative oxygen atom to one water molecule will Attract the
slightly positive hydrogen atom of other water molecule in a weak
electrostatic attraction called hydrogen bond.
 Importance of Water/ Properties of water
 Water is a polar solvent because it is a polar molecule, many ionic
substance like NaCl will dissolve in it. Many covalently bonded substance
are also polar and will dissolve in water but often do not dissolve in other
covalent bonded solvents , such as ethanol. Water also carries other
substance such as starch. Most of the chemical reaction within the cell
occur in water.
 Water is an excellent transport medium because the dipole nature of
water enables many different substances to dissolve in it.
 Water is a liquid so it cannot be compressed.
 Water molecules are cohesive-the forces between the molecules mean they
stick together.
 Water molecules are adhesive- they are attracted to other different
molecules.
 Water is slow to absorb and release heat. It has a high specific heat
capacity.
 Water has a very high surface tension because the attraction between the
water molecules, including hydrogen bonds is greater than the attraction
between water molecule and air.
 As water cools to 4ᴼC, it reaches its maximum density. As it cools further,
the molecules become more widely spaced. As a result, ice is less dense than
water and floats, forming an insulating layer and helping to prevent the
water underneath it from freezing.
Explain how water is involved in the transport
of molecules in living organisms
Water is a ‘universal solvent’ due to the polarity of its
molecules. when sodium chloride (NaCl) dissolves in
water, it produces positive sodium ions and negative
chlorine ions. The positive atoms in water attract the
negative chlorine ions, and the negative atoms
attract the positive sodium ions. All polar substances
can dissolve in polar solvents, such as water. All the
essential substances for living organisms (vitamins,
salts, amino acids, gases, and glucose) transport
inside their bodies in the form of solutes dissolved in
water. These substances take part in metabolic
reactions inside the cells.
 Chemical test for carbohydrate
Starch Test
 Put food sample in a test tube.
 Small amount of water is added in the test tube.
 Add drops of iodine solution to the food sample.
 If starch is present a positive test will show a color change from brown to blue-black
Benedict Solution Test / Reducing Sugar Test
 Small amount of food sample is taken into a test tube. Small amount of water is
added into the test tube.
 Add Benedict’s solution (blue) into sample solution in test tube
 Heat at 60 – 70 °c in water bath for 5 minutes
 Take test tube out of water bath and observe the color.
 If reducing sugar such as glucose is present , A positive test will show a color
change from blue to brick red.
 (color sequence – blue > green > yellow > orange > brick red )
 Biuret test for proteins
 Place food sample into a test tube or 1 cm3 if the sample is
liquid. Add about 1 cm3 depth of water to the tube and stir to
mix.
 Add an equal volume of potassium hydroxide solution to the
tube and stir.
 Add two drops of copper sulfate solution and stir for two
minutes.
 Record the colour of the solution. Proteins are detected
using Biuret reagent. This turns a purple colour when mixed
with protein.
 Spot test-3
15 marks 15 minutes
1. (a) Complete the table below describing the different levels of protein structure
(primary, secondary, tertiary, or quaternary structure). (4)

(b) Amino acids contain a residual or R group. Describe how the R group can affect the
structure of a protein. (4)
(c) Explain, using examples, why globular proteins are more metabolically active than
fibrous proteins. (4)
(d) In the table below give three structural differences between the molecules of
collagen and haemoglobin. (3)
 Iodine test for starch
 Method:
 Place one spatula of the food sample on a dish or 1
cm3 if the sample is liquid.
 Using a dropper, place a few drops of iodine solution
onto the food.
 Record any change in the colour of the solution.
 Starch is detected using iodine solution. This
turns blue-black in the presence of starch.