Post Translational Modifications, protein Targetting And Collagen Biosynthesis Flashcards

1
Q

How many helixes are on collagen

A

3
Every third amino acid would be glycine
Also large amount is Serine and proline

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2
Q

Where are the hydrogen bonds and why would then be there

A

Within the helix structure
Would allow increased stability in the molecule

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3
Q

What would be needed for hydroxylation

A

Vitamins c

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4
Q

What does hydroxylation help with

A

Thermostability

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5
Q

What are the two terminals that’s would be found within the procollagen

A

N terminal
C terminal

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6
Q

What terminal would have the disulfide bonds

A

The C terminal

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7
Q

What causes scurvy and what are some of the symptoms

A

Deficiency of vitamin c or ascortic acid
Weakness, poor healing, gum disease, anaemia

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8
Q

What is osteogenesis imperfecta

A

The mutation in the COL1A1 or COL1A2 genes
Would have glycine substituted for a bulkier amino acid
Not having the correct folding of the molecule

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9
Q

What is elders-Danlos syndrome

A

Stretchy skin
Mutation in the collagen type V or deficiency in the Lysyl oxidase enzymes (not allowing the cores bridges to form)
Would effect the extra cellular cleavage, the cross link formation and stability would be effected

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10
Q

What are the steps that would allow the formation of the cross bridges

A

Lysine residues
Lysyl oxidase and oxygen forming the aldehyde derivatives
Formation of the Aldo’s cross links (thought to be spontaneous)

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11
Q

What cleaves the terminals on pro-collagen to form tropocollagen

A

Collagen peptidase

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12
Q

What is needed for collagen to enter the endoplasmic reticulum

A

The signalling function that would soon be cleaved off (signal pepsidase)

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13
Q

What stages would occur I the extracellular

A

Cleavage of the n and c terminals to for tropocollagen
The formation of the cross bridges

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14
Q

How would preproinsulin go to proinsulin

A

Cleavage of the signalling function
Formation of the disulfide bonds

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15
Q

How would proinsulin go to insulin

A

The cleavage of the C-terminal in the Golgi apparatus

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16
Q

What enzyme is used for the formation of the disulfide bonds

A

Protein disulphide isomerase

17
Q

How can the formation of the disulphide bonds be seen as a redox reaction

A

At first the substrate would be reduced (contains H+) the enzyme would be oxidised.
When the bond formed the substrate would be oxidised as would lose H+ but the enzyme would be reduced as would gain the H+ from the substrate

18
Q

What happens when a protein is misfolded and why

A

Move to the cytosol and would be degraded
If not would build, making it toxic
Damage of the ER

19
Q

How would proteins move into the cells from free ribosomes

A

Signalling element on amino acids (SKL- serine, lysine, leucine)
Attaches to the receptor PTSIR (cytosolic protein receptor)
Would attach to the protein tetramer
Move it to the membrane receptor protein (pex14p)
PTSIR and the tetramer would then move through the membrane
Complex released and the PTSIR moves out (by atp hydrolysis)
Reused

20
Q

How would proteins enter the ER across the membrane

A

The ribosome would attach to the SRPs (signal receptor proteins) these are GTPS
Attaches to another SRP on the membrane
The ribosome soon released (GTP GOES TO GDP AND PI)
This allows the translocon to open
Signal function cleaved off (signal peptidase)

21
Q

What would change if a protein was being made FOR the membrane

A

Added a signal anchor transfer sequence

22
Q

What is O-linked glycosylation

A

Sugar would be added to the OH group of serine of Theronine

23
Q

What is N-linked glycosylation

A

The sugar would be added to the amino acid (asparagine)

24
Q

What are the four things required for protein sorting

A

Signalling function
Receptor
Translocation machinery
The energy (ATP)

25
Q

What re the functions of the endoplasmic reticulum

A

Hydroxylation
Glycosylation
Proper folding of the protein
Insertion of the protein into the membrane
Protein cleavage

26
Q

What can cause protein misfolding

A

Mutation
Protein incorrectly associated with a subunit
Protein can also get stuck in its misfolded form

27
Q

What are the functions of the chaperones

A

Monitor the misfolding
Increase transcription of the chaperones
Decrease translation of the protein
Retain the misfolded protein on the ER

28
Q

What is the difference between the Cis face and the Trans face of the Golgi

A

Cis face is the side closest to the ER and the nucleus
Trans face is the side that is the closest to the membrane of the cell

29
Q

How would the level of C terminal cleaved be different in diabetics

A

Would be low
Diabetics would not produce their own insulin
So would not have a lot of the cleaving of the C terminal

30
Q

What is the difference between PEX14 and PTS1R

A

Both would be used for the transport of a protein into the membrane
PEX14 would be the receptor on the perioxisome
PTS1R would be the complex that would recognise the signalling sequence (SKL in the case of catalase) and carry the protein through the membrane

31
Q

What protein does the SKL (serine leucine lysine) sequence refer too

A

Catalase

32
Q

Why is important glycosylation

A

Protein stability
Protein folding
Deficiency in N-linked (one the amine of asparagine) would lead to inherited diseases (congenital disorders or glycosylation)
Allows interaction with other proteins

33
Q

Where does N-linked glycosylation happen

A

In the ER

34
Q

Where does O-linked glycosylation happen

A

In the golgi

35
Q

What amino acids normally undergo hydroxylation

A

Lysine and proline (in the ER)
Can form proline hydroxylase