Protein Regulation Flashcards

1
Q

What are the methods of protein localisation

A

Temporal and spatial (when and the quality)
Post transcriptional modifications
Scaffolding complexes (making a larger complex)
Specific localisation (creating a protein for a specific area)

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2
Q

Why would ph need to be controlled

A

A certain ph would be needed for specific environments and to activate the protein
If not would have bonds break, domains released and the inactivation (no more translation)

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3
Q

What are protein domains

A

Areas of he protein that would allow the protein to carry out a specific function
For example camodulin (able to form calcium camodulin when smooth muscle contraction occurs)

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4
Q

How would atp be used for the movement of molecules

A

When atp hydrolysed to ADP and pi would allow the movement

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5
Q

How would ATP allow the opening and closing of the channels

A

ATP attached closes opens the channel
ATP hydrolysed to ADP and Pi would close the channel

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6
Q

What are the components of the Rho GTPase and what do they do

A

GAP: converts GTP to GDP (inactivated)
GEF: converts GDP to GTP (activation)
GDI: attached to the Other Rho GTPase molecules and allows them to remain inactive

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7
Q

What would happen if the levels of GEF were low

A

No converstion of GDP to GTP
The levels of GAP would remain high
Lots of GTP to GDP
Would have inactivation

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8
Q

What would happen if the levels of GAP were low

A

No GTP to GDP
Large levels of GEF still
Lots of GDP to GTP
Constant activation

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9
Q

What would phosphorylation and what would dephosphorylate

A

Protein kinase: phosphorylation
Protein phosphatese: dephosphorylates

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10
Q

What amino acids can be phosphorylated

A

Seronine
Theronine
Tyrosine

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11
Q

What are the two ways that active muscle glycogen phosphorylase can be produced

A

By AMP addition
By phosphorylation (phosphorylase kinase which would need ATP energy)

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12
Q

What would be needed for phosphorylation

A

ATP energy

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13
Q

What lysine group would be needed for protein ubiquination

A

Lysine 48

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14
Q

What lysine group would be needed for DNA repair

A

Lysine 63

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15
Q

How would a proteasome work

A

Regulatory region would attach to the protein that would need to be degraded (atp)
Proteasome complex formed
Protein degraded

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16
Q

Where would cAMP bind to on the inactive protein kinase to activate it

A

The regulatory region
Releases the catalytic region
Allows activation and therefore phosphorylation

17
Q

What are the stages in Scr kinase protein regulation

A

Dephosphorylation of region SH2
Ligand would then be bound to the SH3 region
Allows the phosphorylation of the tyrosine amino acid and so activation

18
Q

What would be the fate of the proteins that undergo lipidation

A

Go to the plasma membrane