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COLLAGEN
Water-insoluble fibers
Primary Structure
-(-XYG-)- XPro/Hyp; Yany aa
- each chain is about 800 aa residues long
Secondary Structure
- Left-handed -helix
- 3.3 aa/turn
- Pitch: 10
Tertiary Structure
- 3 chains are parallel & wind each other in a right-handed manner to form a
triple-helical structure
- H-bond involving Hyp and Hyl residues
- intramolecular and intermolecular aldol covalent crosslinks
Quaternary Structure
Procollagen Tropocollagen Collagen Fibrils
Diseases due to Collagen Defects
1. Scurvy deficiency in ascorbic acid (requirement for the activity of prolyl
hydroxylase)
2. Ehlers-Danlos Syndrome India-rubberman
ELASTIN
Hemeproteins
Major role:
Hemoglobin: O2 transport
Myoglobin: O2 storage
Heme
Prosthetic group
Porphyrin ring
Centrally bound Fe+2
MYOGLOBIN
Monomer
Contains a heme
10 Structure: 153 aa
20 Structure: Helical
30 Structure: Globular
HEMOGLOBIN
Tetramer: 22
10 structure
= 141 aa
= 146 aa
20 structure: helical
30 structure: globular
Oxyhemoglobin
Carbaminohemoglobin
Carboxyhemoglobin
Methemoglobin
Sickle-Cell Anemia
Regulatory proteins
Endocrine hormones
Insulin: B cells
Glucagon: A cells
Carbohydrate homeostasis
Insulin
Hypoglycemic hormone
Glucagon
Hypoglycemia
Hyperglycemia
Diabetes mellitus
IMMUNOGLOBULIN
Defense proteins
Structure
Y-shaped molecule
Tetramer
Light Chain
Heavy Chain
Constant Region
Variable Region
Autoimmune Diseases
Inherited Immunodeficiency
HIV