Proteins
Proteins
Proteins
Protein Structure
1. Primary Structure
2. Secondary structure
• Most common types are @helix and Beta- pleated sheet which are
stabilized by H-bond between carbonyl and N-H groups.
@-Helix
• In almost all proteins, the helical twist of the helix is right handed.
• There are 3.6 amino acid residues per turn of the helix and the pitch
is 0.54 nm. Each residue from other is separated by 1.5 A° (0.15
nm).
• The proline tends to disrupt @-helices because it lacks -NH group and
because its ring structure restricts its value near 60°
B pleated sheets
• The Antiparallel -sheets are more stable than parallel because fully
B
colinear H-bonds form.
3. Tertiary Structure
D
4. Quaternary Structure
• Non-Covalent Interactions -
1. Hydrophobic
2. Electrostatic (salt bridges)
3. Hydrogen bonds
• Covenlent Interactions -
1. Interchain disulphide bond
Denaturation of Proteins
• Denaturation of proteins is the loss of native conformation. It means
loss quaternary, tertiary and secondary structure of proteins.
1. Effect of pH
• Above and below the pI causes for increase in the -ve and +ve charge
molecule respectively and therefore creates repulsion.
• The simple proteins contain only amino acids. eg; Serum Albumin
IT
Fibrous and Globular Proteins
Ei
Collagen
• The chain are left handed polypeptide helices having 3.3 amino
acid residues per turn that wind around one another in characteristic
right-handed triple helix.
• The 25 different kinds of a chain forms 19 different collagen
molecules (Type - I, II, and III → 90% collagens).
Structure
• The glycine = approx. 1/3 of amino acid residue. And proline and
hydroxyproline causes for the rigidity of collagen.
• The x chain are synthesized on RER's ribosomes and enter its lumen.
I
Elastin
Pathway
Keratin
Distal
Histidine
N
n
Proximal
Histidine
2. HbA2 (
9282) - Contains 2 8 and 2 X chains. Makes 2% of adult
Hb.
Oxygen Transport
2. Relaxed (R) - The oxygen binds with higher affinity in this state.
• The binding of 1st oxygen molecule with deoxy state occurs weakly,
because it binds to a subunit in T state and starts a conformational
change.
• The last (4th) oxygen molecule binds to heme in a R state subunit with