W2- Lecture 10- Post-translational Modifications Of Proteins Flashcards

1
Q

Over what no of amino acids can a poly pep time fold into a defined shape ?

A

40 AA

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2
Q

Primary secondary’s and tertiary structure of proteins

A

1- sequence of aa
2- interaction between aa e.g alpha helixes or beta sheets , loops and coils
3- 3D shape
4 - more then one protein = complex

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3
Q

What direction / terminus do we read

AA form/to ?

A

N terminus to the C terminus

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4
Q

What mutation causes sickle cell disease ?

A

mutation in hba haemoglobin/ beta globin gene sunbsitation from T to A
Glu to val
Side chain changes which causes impact

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5
Q

Where can we find the ionic bonds / electrostatic attraction ?

A

In the r group between

CO2- and NH3+

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6
Q

Where can we find the disulfide bridges ?

A

Between cysteine and SH Groups

Cys-S-S-Cys

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7
Q

What are proproteins?

A

Inactive proteins that need activation before use

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8
Q

Where is the preproinsulin fed from / into ?

A

Ribosomes feed into ER

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9
Q

Name the three steps of post translational modification of proinsulin
+ where

A
All in ER 
1- Cleavage and removal of signal peptides 
2-Oxidation of SH groups to SS
(disulfide bridge formation )
3- Cleavage and removal of the C chain
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10
Q

Why is post translational mod of proteins important ?

A
  • to allow proteins to have a different spacial arrangement / biological activity
  • allows regulation of proteins
  • Increases protein diversity
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11
Q

Name different PTM

A

Cleavage
isomerism
Addition of Small molecules e.g phosporylation

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12
Q

Describe protein phosphorylation

A

Phosphate group donated by ATP

Catalysed by protein kinase

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13
Q

What enzyme catalysed the back reaction of phosphorylation of a protein ?

A

Phosphatase

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14
Q

Describe how pyruvate dehydrogenase is regulated by phosphorylation/ de phosphorylation

A

phosphorylation/ de phosphorylation is regulated by protein kinase

Activated by high NADH and AcetylCoA

but inhibited by pyruvate

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15
Q

Explain how EGF receptor binds with ligand and how phosphorylation takes place + impact

A
  • when binds to ligand
  • forms firmer
  • phosphorylation each other
  • activates of genes- can lead to excess cell growth
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16
Q

What is the cell cycle dependant on ?

A

Cyclin and cyclin dependant kinases

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17
Q

How do Cyclin and cyclin dependant kinases act to promote the cell cycle

A

CDK and cyclins only work when boundtogether

  • CDKs phosphorylate serine is threonine
  • promotes cycle from moving to the next step in the cycle
  • type of cyclin and concentration drive cell cycle
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18
Q

What are the two most phosphorylated AA?

A

Serine

Threonine (often associated with each other)

19
Q

What does tyrosine phosphorylation cause ?

A

Activation off signalling networks but activator gets protein protein interactions

20
Q

Detecting phosphorylated proteins

A

Phospho-specific antibodies

2d electrophoresis + western blotting

21
Q

describe protein acetylation

A

Acetyl group is donated by acetyl Coenzyme A to a lysine

Catalysed by protein acetyltransferase (PAT)

22
Q

Describe the deacetylation of a protein

A

Catalysed by protein DeACetylase (PDAC)

Where an acetyl group is removed from the amino acid lysine within a protein

23
Q

Where is the primary target for acetylation

24
Q

Describe protein methylation

A

Methyl group donated by S-adenosylmethionie
Catalysed by protein methyl transferase
Majorly arginine and lysine
Not all reversible

25
Describe demetthylation of a protein
Methyl group removed Catalysed by protein demethylase Majorly arginine and lysine Not all reversible
26
What is the histone code hypothesis
That multiple histone modifications will lead to specific down stream effects
27
Describe a way PTM changing chemical nature of AA
Citullination/deimination Of arginine converting it to citrulline Positive charge to neutral charge Immune system attacked citrullinated proteins Causing autoimmune response and arthritis
28
Explain glycosilation
Addition. Of mono/polysaccarides or other proteins After glycosylation = glycoprotein Effects folding
29
Name two important AA that are glycosylated for the cell surface structure
Asparagine - linked (N) | Or serine/Threonine- linked (o)
30
Where does glycosylation take place
N linked ER O linked in the golgi / cytoplasm
31
Describe n linked glycosylation
Polysaccaride added as a 14 sugar subunit to asparagine In the ER
32
DESCRIBE O linked glycosylation
Sugar added one at a time In golgi (secreted p)/ cytoplasm (cellular p ) Sugar added to hydroxyl group of serine or threonine Rarely lysine or hydroproline are glycosylated
33
How is the n linked oligosaccrides processed ?
Er - removes 3 glucose residues Golgi - mannose residues removed + other sugars added
34
Protein ubiquination | +aim
``` Ubiquity attached its glycine to lysine Needs 3 enzymes Ubiquitous activating enzymes Ubiquitous conjugating Ubiquitous ligand (E1 , E2 , E3) Marked for degradation in a proteasome (regulating proteins ) ```
35
Which enzyme removed ubiquitin from its attachment protein ?
Deubiquitinating enzyme (DUBs)
36
Protein control everything - so by controlling it via ubuquitantion
You can control e.g synaptic transmission
37
Name 4 types of lipidation Aka increasing affinity to lipids
C-terminal glycosyl phosphatidylin (GPI)anchor N terminal myristoylation S-myristoylation S-prenylation (These aren’t mutally exclusive )
38
GPCR Regulation via phosphorylation
Phosphorylation action on protein which recycles receptor to cell surfaces or Can be degraded
39
Name two PTM that modify the amino acids | Reversible ?
Deamination Eliminylation Irreversible
40
Name 1 PTM that causes cleavage | Reversible?
Proteolysis | Irreversible
41
Name 2 PTM that add polypeptides | Reversible ?
Ubiquitylation UBL- protein conjugation Yes reversible
42
Name 4 PTM that add complex molecules | Reversible ?
AMPlyation ADP-ribosylation Glycosylation Isoprenylation Reversible
43
Name 3 PTM that add chemical groups | Reversible ?
Hydroxylation Phosphorylation Acetylation Methylation Reversible