451069
Beschreibung
Quiz von gina_evans0312, aktualisiert more than 1 year ago
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Erstellt von gina_evans0312
vor etwa 11 Jahre
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Frage 1
Frage
Chaperonins are for nascent proteins that don't fold independently or interact with other cytosolic chaperones
Antworten
- True
- False
Frage 2
Frage
To what is the arrow pointing on the Gro-El monomer?
Antworten
-
Apical substrate binding site
-
Hinge
-
ATP binding site
Frage 3
Frage
How many monomers make up Gro-El?
Antworten
-
14- 7 in each layer
-
12- 6 in each layer
-
10- 5 in each layer
Frage 4
Frage
Gro-Es is made of 7 monomers
Antworten
- True
- False
Frage 5
Frage
Why does Gro-Es bind to close the cavity?
Antworten
-
Creates a space away from crowded cytosol for protein binding
-
Creates a highly acidic environment for proteins to fold in
-
Allows protein to fold in highly saline environment
Frage 6
Frage
ATP & Gro-Es bind at separate points in the protein folding cycle
Antworten
- True
- False
Frage 7
Frage
The nascent protein will bind at the monomer level _ side with ADP and Gro-Es bound
Antworten
-
At the same
-
Opposite
Frage 8
Frage
Once Gro-Es and ATP are bound, the protein refolds for _ seconds whilst the ATP is hydrolysed
Antworten
-
10-15
-
15-20
-
20-25
Frage 9
Frage
When the protein has folded properly, what happens?
Antworten
-
A nascent polypeptide binds to the end opposite the Gro-Es and ADP, causing the cycle to repeat itself at the other end of the protein
-
Gro-Es dissociates, releasing the folded protein
-
The ADP is released and replaced with ATP
Frage 10
Frage
The CCT and Gro-El cycles are basically the same, but Gro-El has flexible extensions that CCT does not
Antworten
- True
- False
Frage 11
Frage
What is bacterial homologue of the Hsp100 family?
Antworten
-
Clp
-
Clr
-
Cld
Frage 12
Frage
Hsp100 and its bacterial homologue are hexamers
Antworten
- True
- False
Frage 13
Frage
Clp100 and its bacterial homologue do what?
Antworten
-
Unfold proteins in the presence of ATP
-
Fold proteins in the presence of ATP
Frage 14
Frage
What is the difference between Class 1 & Class 2 Hsp100 proteins?
Antworten
-
Class 1- Protein degredation Class 2- Protein disaggregation and refolding
-
Class 1- Protein disaggregation and refolding Class 2- Protein degredation
Frage 15
Frage
How do you tell apart Class 1 and Class 2
Antworten
-
Class 1 has 2 ATPase sites, Class 2 has 1
-
Class 1 has 1 ATPase site, Class 2 has 2
Frage 16
Frage
Hsp100's consist of one/two sets of hexamers
Antworten
- True
- False
Frage 17
Frage
The ATP is hydrolysed in Hsp100's/Clp proteins to allow what?
Antworten
-
To drive conformational changes in aromatic loops that interact with the substrate
-
To provide energy to break the peptide bonds in the protein to be unfolded
-
To provide energy to posh apart poorly stacked peptides
Frage 18
Frage
When ClpA and ClpP interact, what is the role of the supercomplex?
Antworten
-
Unravel denatured protein
-
Refold it
-
Degrade it
Frage 19
Frage
Hsp90 chaperones are required for what?
Antworten
-
High temperature growth
-
High salinity growth
-
High pH growth
Frage 20
Frage
Hsp90 are ATP dependent monomers
Antworten
- True
- False
Frage 21
Frage
What is found on the N-terminus of a Hsp90 protein?
Antworten
-
ATP binding site
-
Substrate binding domain
-
Dimerisation domain
Frage 22
Frage
The dimerisation domain of Hsp90 occurs at the C terminus
Antworten
- True
- False
Frage 23
Frage
ATPase inhibitors of Hsp90 target which part of the protein?
Antworten
-
N terminus
-
C terminus
-
Middle
Frage 24
Frage
The binding of ATP causes the ATP 'lid' to close and the dimer to split
Antworten
- True
- False
Frage 25
Frage
Name the conformational changes that occur after ATP binds
Antworten
-
N-terminals undergo Beta strand exchange
-
N-terminals undergo Alpha helix exchange
-
Rotation of N domain (relative to middle) to allow meeting of dimerisation domains
-
Rotation of C domain (relative to middle) to allow meeting of dimerisation domains
Frage 26
Frage
What is the role of the core domain of Hsp90 (with regards to the ATPase)
Antworten
-
It's flexible enough that it completes the dimerisation site and allows ATP hydrolysis to occur
-
It's flexible enough that it completes the ATPase site and allows ATP hydrolysis to occur
-
Interacting with the gamma phosphate of ATP
Frage 27
Frage
The conformational changes of Hsp90 are thought to be brought about by client proteins
Antworten
- True
- False
Frage 28
Frage
cd37/p50 inhibit Hsp90 by what process?
Antworten
-
Binding it to Hsp70
-
Preventing N-terminal dimerisation
-
Phosphorylation of Hsp90
Frage 29
Frage
Sti/HOP bind to the N-terminal of Hsp90 & Hsp70, binding them together as a potent inhibitor
Antworten
- True
- False
Frage 30
Frage
Aha activates Hsp90 how?
Antworten
-
Activates ATPase activity by promoting open state of of catalytic loop
-
Causing N-terminal alignment for dimerisation
-
Physically holding the active site open
Frage 31
Frage
Spa1 both inhibits and stimulates ATPase activity, leading to an overall slowing of ATPase in Hsp90
Antworten
- True
- False
Frage 32
Frage
How does Sba activate ATPase activity?
Antworten
-
Interacts with the middle domain of Hsp90 and modulates the catalytic loop of this domain
-
Increases the affinity of the dimerisation sites for each other, completing the ATPase sites more stably
-
Increases the affinity for the binding site for ATP
Frage 33
Frage
Hsp90 can be used to activate steroid receptors and kinases
Antworten
- True
- False
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