451069
Descrição
Quiz por gina_evans0312, atualizado more than 1 year ago
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Criado por gina_evans0312
mais de 10 anos atrás
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Questão 1
Questão
Chaperonins are for nascent proteins that don't fold independently or interact with other cytosolic chaperones
Responda
- True
- False
Questão 2
Questão
To what is the arrow pointing on the Gro-El monomer?
Responda
-
Apical substrate binding site
-
Hinge
-
ATP binding site
Questão 3
Questão
How many monomers make up Gro-El?
Responda
-
14- 7 in each layer
-
12- 6 in each layer
-
10- 5 in each layer
Questão 4
Questão
Gro-Es is made of 7 monomers
Responda
- True
- False
Questão 5
Questão
Why does Gro-Es bind to close the cavity?
Responda
-
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
Questão 6
Questão
ATP & Gro-Es bind at separate points in the protein folding cycle
Responda
- True
- False
Questão 7
Questão
The nascent protein will bind at the monomer level _ side with ADP and Gro-Es bound
Responda
-
At the same
-
Opposite
Questão 8
Questão
Once Gro-Es and ATP are bound, the protein refolds for _ seconds whilst the ATP is hydrolysed
Responda
-
10-15
-
15-20
-
20-25
Questão 9
Questão
When the protein has folded properly, what happens?
Responda
-
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
Questão 10
Questão
The CCT and Gro-El cycles are basically the same, but Gro-El has flexible extensions that CCT does not
Responda
- True
- False
Questão 11
Questão
What is bacterial homologue of the Hsp100 family?
Responda
-
Clp
-
Clr
-
Cld
Questão 12
Questão
Hsp100 and its bacterial homologue are hexamers
Responda
- True
- False
Questão 13
Questão
Clp100 and its bacterial homologue do what?
Responda
-
Unfold proteins in the presence of ATP
-
Fold proteins in the presence of ATP
Questão 14
Questão
What is the difference between Class 1 & Class 2 Hsp100 proteins?
Responda
-
Class 1- Protein degredation Class 2- Protein disaggregation and refolding
-
Class 1- Protein disaggregation and refolding Class 2- Protein degredation
Questão 15
Questão
How do you tell apart Class 1 and Class 2
Responda
-
Class 1 has 2 ATPase sites, Class 2 has 1
-
Class 1 has 1 ATPase site, Class 2 has 2
Questão 16
Questão
Hsp100's consist of one/two sets of hexamers
Responda
- True
- False
Questão 17
Questão
The ATP is hydrolysed in Hsp100's/Clp proteins to allow what?
Responda
-
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
Questão 18
Questão
When ClpA and ClpP interact, what is the role of the supercomplex?
Responda
-
Unravel denatured protein
-
Refold it
-
Degrade it
Questão 19
Questão
Hsp90 chaperones are required for what?
Responda
-
High temperature growth
-
High salinity growth
-
High pH growth
Questão 20
Questão
Hsp90 are ATP dependent monomers
Responda
- True
- False
Questão 21
Questão
What is found on the N-terminus of a Hsp90 protein?
Responda
-
ATP binding site
-
Substrate binding domain
-
Dimerisation domain
Questão 22
Questão
The dimerisation domain of Hsp90 occurs at the C terminus
Responda
- True
- False
Questão 23
Questão
ATPase inhibitors of Hsp90 target which part of the protein?
Responda
-
N terminus
-
C terminus
-
Middle
Questão 24
Questão
The binding of ATP causes the ATP 'lid' to close and the dimer to split
Responda
- True
- False
Questão 25
Questão
Name the conformational changes that occur after ATP binds
Responda
-
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
Questão 26
Questão
What is the role of the core domain of Hsp90 (with regards to the ATPase)
Responda
-
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
Questão 27
Questão
The conformational changes of Hsp90 are thought to be brought about by client proteins
Responda
- True
- False
Questão 28
Questão
cd37/p50 inhibit Hsp90 by what process?
Responda
-
Binding it to Hsp70
-
Preventing N-terminal dimerisation
-
Phosphorylation of Hsp90
Questão 29
Questão
Sti/HOP bind to the N-terminal of Hsp90 & Hsp70, binding them together as a potent inhibitor
Responda
- True
- False
Questão 30
Questão
Aha activates Hsp90 how?
Responda
-
Activates ATPase activity by promoting open state of of catalytic loop
-
Causing N-terminal alignment for dimerisation
-
Physically holding the active site open
Questão 31
Questão
Spa1 both inhibits and stimulates ATPase activity, leading to an overall slowing of ATPase in Hsp90
Responda
- True
- False
Questão 32
Questão
How does Sba activate ATPase activity?
Responda
-
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
Questão 33
Questão
Hsp90 can be used to activate steroid receptors and kinases
Responda
- True
- False
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