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1.4 Proteins-1
1.4 Proteins-1
1.4 Proteins-1
4 Protein
At the end of the lesson, student should be able to
explain:
a. Describe the basic structure of amino acid
b. State how amino acids are grouped
c. Describe primary(10), secondary(20), tertiary(30) and
quaternary(40 ) levels and types of bonds involved
d. Describe the effect of pH and temperature on the
structure of protein
e. Explain the formation and breakdown of dipeptide
f. Classify proteins according to their structure &
compoosition
1.4 Protein
• Proteins contain the elements carbon,
hydrogen, oxygen and nitrogen
• Many proteins contain sulfur and phosphorus
• Proteins are built up from more than one
amino acids.
• Amino acid is a monomer of protein.
Learning Outcomes :
1.4 (a) Describe the basic structure of amino acids
H
Learning Outcomes :
Learning Outcomes :
1.4 (a) Describe the basic structure of amino acids
1.4 (a) Describe the basic structure of amino acids
2 functional groups:
i. COOH (carboxyl group) : acidic
ii. NH2 (amino group) : basic
Amino acids are amphoteric; have both acidic &
basic properties
R
H
Group of Amino acid
pleated sheet
+H N
3 Examples of
Amino
amino acid
end
subunits
helix
α- helix
1. Primary structure
Primary Structure
Linear polypeptide is a
linear sequence of amino H3 N
+
β- pleated sheet
Secondary Structure
pleated sheet
Examples of
amino acid
subunits
helix
3. Tertiary Structure
side chains
Ionic bond
3. Tertiary Structure
Hydrophobic
3. Disulphide bridge interactions and
van der Waals
covalent bond that form interactions
when 2 amino acids with Polypeptide
sulfhydryl groups (-SH) on backbone
their side chains Hydrogen
bond
4. Hydrophobic interactions
Disulfide bridge
& van der Waals forces
Nonpolar R group with
another nonpolar R group
Ionic bond
Fig. 5-21f
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
FIGURE:
4 types of bond that maintained
the tertiary structure of protein
Tertiary Structure
4. Quaternary structure
Example: Hemoglobin
that carries oxygen
contains four globular
polypeptide chains
Two alpha (α) two beta
(β) polypeptide chains
Each containing a haem
group with an iron atom
that can bind with a
single oxygen molecule.
Fig. 5-21g
Polypeptide Chains
chain
Iron
Heme
Chains
Hemoglobin
Collagen
Factor affecting the structure of protein
condensation
+ H2O
+ H2O hydrolysis
Condensation
reaction
Hydrolysis
reaction
1. Fibrous Protein
2. Globular Protein
3. Conjugated Protein
Properties of fibrous protein
i. Fibrous protein
1. Long parallel polypeptide chains.
2. Protein structural level is secondary
structure.
3. Maintain by hydrogen bond only.
4. Stable structure
5. Insoluble in water
6. Eg: Keratin, actin, myosin, collagen, silk
Properties of globular protein
• Globular proteins
1.Polypeptide chains folded or spherical shape
2.Protein structural level is tertiary or
quaternary structure
3.Maintain by ionic bond, disulfide bridge,
hydrophobic interaction and van de Waals
interaction
4. Relatively unstable structure
5. Soluble in water(can form colloid)
1. Conjugated Protein