Chaperonins

Question

Chaperonins are for nascent proteins that don't fold independently or interact with other cytosolic chaperones

Answer 1

Apical substrate binding site

Answer 2

ATP binding site

Answer 3

14- 7 in each layer

Answer 4

12- 6 in each layer

Answer 5

10- 5 in each layer

Answer 6

Creates a space away from crowded cytosol for protein binding

Answer 7

Creates a highly acidic environment for proteins to fold in

Answer 8

Allows protein to fold in highly saline environment

Answer 9

At the same

Answer 10

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

Answer 11

Gro-Es dissociates, releasing the folded protein

Answer 12

The ADP is released and replaced with ATP

Answer 13

Unfold proteins in the presence of ATP

Answer 14

Fold proteins in the presence of ATP

Answer 15

Class 1- Protein degredation Class 2- Protein disaggregation and refolding

Answer 16

Class 1- Protein disaggregation and refolding Class 2- Protein degredation

Answer 17

Class 1 has 2 ATPase sites, Class 2 has 1

Answer 18

Class 1 has 1 ATPase site, Class 2 has 2

Answer 19

To drive conformational changes in aromatic loops that interact with the substrate

Answer 20

To provide energy to break the peptide bonds in the protein to be unfolded

Answer 21

To provide energy to posh apart poorly stacked peptides

Answer 22

Unravel denatured protein

Answer 23

Degrade it

Answer 24

High temperature growth

Answer 25

High salinity growth

Answer 26

High pH growth

Answer 27

ATP binding site

Answer 28

Substrate binding domain

Answer 29

Dimerisation domain

Answer 30

N terminus

Answer 31

C terminus

Answer 32

N-terminals undergo Beta strand exchange

Answer 33

N-terminals undergo Alpha helix exchange

Answer 34

Rotation of N domain (relative to middle) to allow meeting of dimerisation domains

Answer 35

Rotation of C domain (relative to middle) to allow meeting of dimerisation domains

Answer 36

It's flexible enough that it completes the dimerisation site and allows ATP hydrolysis to occur

Answer 37

It's flexible enough that it completes the ATPase site and allows ATP hydrolysis to occur

Answer 38

Interacting with the gamma phosphate of ATP

Answer 39

Binding it to Hsp70

Answer 40

Preventing N-terminal dimerisation

Answer 41

Phosphorylation of Hsp90

Answer 42

Activates ATPase activity by promoting open state of of catalytic loop

Answer 43

Causing N-terminal alignment for dimerisation

Answer 44

Physically holding the active site open

Answer 45

Interacts with the middle domain of Hsp90 and modulates the catalytic loop of this domain

Answer 46

Increases the affinity of the dimerisation sites for each other, completing the ATPase sites more stably

Answer 47

Increases the affinity for the binding site for ATP

Siguiente

Chaperonins

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	Creado por gina_evans0312 hace más de 10 años