Endocytosis and Protein Degredation Flashcards

1
Q

What does Hsp70 do?

A

Binds to protein as it is being made and helps fold protein.

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2
Q

What does hsp60 do?

A

It binds protein after synthesis and then uses ATP to relax the protein and allow it to refold.

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3
Q

How does the cell know if a protein is properly folded?

A

UGGT (UDP-glucose:glycoprotei glucosyl transferase) recognizes it and its something we don’t understand completely.

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4
Q

What marks a protein for degradation?

A

Ubiquitin.

Ubiquitin also does other things.

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5
Q

How many ubiquitins are needed to degrade a protein?

A

4 or more

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6
Q

Which subunit of the proteasome cleaves hydrophobic AA?

A

B5 Chymotrypsin-like (Hydro has 5 letters in it)

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7
Q

Which subunit of the proteasome cleaves basic AA?

A

B2- trypsin like- “B”asic

2nd letter in the alphabet

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8
Q

Which subunit of the proteasome cleaves acidic AA?

A

B1 Caspase like- “A”cidic.

A is the first letter in alphabet

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9
Q

Patients with which disease are immune to ebola?

A

Niemann-Pick

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