Session 9-Collagen Flashcards

1
Q

What is the basic unit of collagen?

A

Tropocollagen

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2
Q

Which AA is in every third position along each alpha chain?

A

Glycine

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3
Q

How many alpha chains is collagen made from?

A

Three

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4
Q

What are the characteristics of the triple helix that forms collagen? (4)

A
  1. Made up of alpha chains but not an alpha helix
  2. Non-extensible
  3. Non-compressible
  4. High tensile strength
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5
Q

Why is glycine so abundant in collagen?

A

Glycine is the only AA with a small enough side chain to fit in the middle of the helix on the inside

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6
Q

Each alpha chain has this repeat: (Gly-X-Y)n.

Which AA are usually found in the X and Y positions?

A

Proline or hydroxyproline (hydroxyproline is not part of the 20 AA, it is formed when Pro is hydroxylated)

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7
Q

Which bonds are found between alpha chains and what do they do?

A

Hydrogen bonds stabilise the structure

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8
Q

How many types of collagen are there?

A

28

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9
Q

What is the 1) molecular formula of type I collagen and 2) what is its tissue distribution?

A

1) Alpha1 (I)2 alpha2 (I)
2) skin
Tendon/ligaments
Bone
90% of all body collagen

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10
Q

What is the 1) molecular formula of type II collagen and 2) what is its tissue distribution?

A

1) alpha1(II)3
2) Cartilage
Intervertebral discs

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11
Q

What is the 1) molecular formula of type III collagen and 2) what is its tissue distribution?

A

1) alpha1(III)3
2) foetal skin
Cardiovascular system

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12
Q

What is the 1) molecular formula of type IV collagen and 2) what is its tissue distribution?

A

1) alpha1(IV)2 alpha2(IV)

2) basement membrane

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13
Q

Why is tropocollagen secreted before final processing occurs?

A

Collagen is large so the cell would burst

Peptidases are only activated outside the cell

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14
Q

What causes scurvy?

A

Weak tropocollagen triple helices due to less vitamin C in the diet so hydrogen bonds cannot form

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15
Q

What does CHADPOGRL stand for?

A
Cleavage of signal peptides
Hydroxylation of proline and lysine
Addition of N-linked oligosaccharide and galactose (in ER)
Disulphide bridge formation 
Procollagen (sent to golgi)
O-linked glycosylation (in golgi)
Golgi-exocytosis as tropocollagen 
Removal of N/C terminal peptides (procollagen peptidase)
Lateral aggregation to form fibrils
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