Introduction to Protein

Mr Koech

DPT Biochemistry
 About Protein
• Protein is a polymer consisting of many amino acids.
• Building blocks of body made up of amino acids
Formation of Peptide Bond
 Cont’
• Process is called Condensation or Dehydration process because water is
lost.

• The resulting is Di-peptide bond because two amino acids combined

 Cont’
• Peptide bond form by end side of carboxyl and amine.

• To form a covalent bond which is hard to break.

 Protein Structure 4 Levels
• Primary
• Secondary
• Tertiary
• Quaternary
 Primary Structure
• Based on sequence of amino acids found on the protein
• The sequence determines the shape of the protein.
• For example below;

• If you change one amino acid, it will completely change the shape and
function of the protein
 Secondary Structure
• Describes the localized shape.
1.Alpha Helix
• Stabilized by Hydrogen bond.

Each turn/bend contains 3.6 residues

of amino acids.

• NH of another interacts with

Carbonyl of another.
 B Pleated sheet
• Alternates and stabilized also by Hydrogen Bond.
 Tertiary Structure
• Represent a complete 3D folding pattern of protein
• Consist of 1 individual sub-unit.
 Quaternary structure
• Comprises of many sub units.
• Hemoglobin consist of
• two alpha helix and Beta Pleated sheet.
 Kinds of Proteins

1.Enzymes
• Catalyzes chemical reactions.

• Source:Dave explains
• 2. Haemoglobin Receptors
• Carries Oxygen Controls signals in the body

Source:Dave explains
Dehydration
• An amide is a functional group with a Nitrogen atom next to
carbonyl and it is the functional group which will connect each
amino acid during polymerization.

• Protein consist of 300-1000 amino acids.

• Protein by convention we write N-terminus on the left and C-
terminus on the right.
• Each monomeric unit of polypeptide is called a residue.
• For alpha helix 3 or 4 amino per turn and R groups pointing out.

• Sigma bond is flexible, di-bond is rigid

Protein Abbreviation
• Tertiary level is a complete folding and specific to protein.
• The shape determines the function
• Factors affecting tertiary level;
• 1.Hdrophobic residues are in the interior.
• 2.Hydrophilic residues found on the surface of protein so that they can
make di-pole-dipole or ion-ion interactions with water molecules.
• 3.Disulfide Bond
Thiol R-SH replaces Oxygen
Thiol oxidation= Disulfide bond
Packed and Long protein folding
• Quaternary level have four sub units of alpha helix and
Beta pleated sheet.
• They are not covalently bond but held by strong
electrostatic interactions.
• Summary:
• Change in amino acid
• The resultant mutation of hemoglobin takes
on different shape which can clog blood
vessels.