Test
Constituative Chaperones
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Preguntas del test (37)
1Which of the following is not a role of the DNAK/Hsp70 superfamily?
- AStabilise nascent polypeptides
- BRepaor heat shocked proteins
- CPreserve folding proteins
- DProtein transport
- EProtein degredation
2Hsp70s (unlike DNAK's) do not require chaperones
- AVerdadero
- BFalso
3What is the role of DNAJ/Hsp40 when combined with DNAK/Hsp70
- AATPases
- BKinases
- CPeptidyl propyl isomerases
4DNAK/Hsp70 need NEF's in order to function
- AVerdadero
- BFalso
5Where is the Hsp70/DNAK binding domain for ATP?
- AN-terminus
- BCore
- CC- terminus
6Name the subdomains of the ATPase found in DNAK/Hsp70
- A1A
- B1B
- C1C
- D2A
- E2B
- F2C
7What increases the ATPase activity of the ATP binding domain?
- AThe binding of the substrate
- BMovement into an acidic compartment
- CDNAJ/Hsp40 binding
- DYDJ1 binding
- ESSA
8The core substrate binding domain has an affinity for what?
- ANeutral, hydrophobic aa
- BAcidic, polar aa
- CBasic, polar aa
9The C-terminus of DNAK/Hsp 70 acts as a 'lid' for the protein
- AVerdadero
- BFalso
10When ATP is hydrolysed in DNAK/Hsp70, where does the C-terminus bind to?
- AThe N-terminus
- BThe core
- CIt doesn't move at all
- DOver the bound substrate
11Without the assistance of DNAJ/Hsp40, the ATPase in DNAK/Hsp70 works too slowly for the C-terminus to trap the bound substrate
- AVerdadero
- BFalso
12Hsp70/DNAK's preferred binding pattern is 15 aa long
- AVerdadero
- BFalso
13What are the 'Flanking' residues (1-4, 9-13) of Hsp70's preferred binding site made of?
- ALeu
- BArg
- CLys
- DTrp
14The preferred residue for the -Core- of Hsp70's preferred binding site is Valine
- AVerdadero
- BFalso
15What other residues can make up the 'core' of the preferred binding site/
- AIle
- BVal
- CPhe
- DTyr
16How does this 'Preferred Binding Patter' for Hsp70 help direct the protein?
- AIn properly folded proteins, the hydrophobic stretch is hidden, and so only nascent/denatured proteins have the exposed residues for Hsp70 to bind to
- BIn nascent/denatured proteins, these hydrophobic residues will be added by Hsp40, so it can recognise them
- CStretches with the core residues are removed during protein folding, so only nascent polypeptides have them
17What is the role of the J domain in a Hsp40?
- AContain the HPD peptide needed to boost Hsp40's ATPase
- BGly/Phe rich linker for positioning
- CDimerisation domain
- DZn+ 'finger' for substrate binding
18The role of the Gly/Phe rich linker does what?
- AMakes DNAJ/Hsp40 flexible enough to bind to its respective protein
- BMakes DNAJ/Hsp40 a more effective ATPase
- CAllows DNAJ/Hsp40 to locate its respective DNAK/Hsp70
19The Zinc 'Finger' is for substrate binding
- AVerdadero
- BFalso
20Which amino acids make up the HPD domain?
- AHistadine
- BProline
- CAspartate
- DLeucine
- EGlycine
21The Znc finger of DNAJ/Hsp40 can interact with the nascent polypeptide and bring it to the DNAK/Hsp70
- AVerdadero
- BFalso
22What is the sequence of the Zinc 'finger'?
- ACXXCXGXG
- BGXXGXCXC
- CGXXCXGXC
- DCXXGXCXG
23The C-terminus of Hsp40 is for tetramerisation
- AVerdadero
- BFalso
24What effect does the GEF factor binding have on the Hsp70/Hsp40 complex?
- AADP is replaced with ATP
- BATP is replaced with ADP
- CHsp40 dissociates
- DNewly folded protein binds
- ENewly folded protein dissociates
25When the substrate & Hsp40 bind to Hsp70, the GEF factor also binds
- AVerdadero
- BFalso
26How is the nascent polypeptide transferred from the DNAJ site to the DNK site?
- AThe G/F domain is flexible enough to bind to the DNAK site and pull it in for transfer
- BThe J domain is pulled like a thread through the ATPase, bringing the two sites close enough together for transfer
- CThe dimerisation of the DNAJ pulls the two sites close together
27In which of the following is Prefoldin found?
- AArchea
- BProkaryotes
- CEukaryotes
28Prefoldin can act as a substitute for Hsp70 if the organsim doesn't have the latter
- AVerdadero
- BFalso
29Prefoldin is ATP dependent
- AVerdadero
- BFalso
30Prefolding is a...
- ADimer
- BTetramer
- CHexamer
31What is the role of Preofoldin in Archea?
- ACaptures nascent polypeptides and binds them to Gro-El
- BCaptures nascent polypeptides and binds them to CCT
- CCaptures nascent polypeptides and binds them to SSA
32In Eukaryotes, prefoldin might be specific for the folding of what?
- AActin/tubulin
- BCCT
- CHsp40
- DHsp70
33In archea there are 6 Prefoldin genes (Grim1-6) in Eukaryotes there are 2 (Gimalpha and Gimbeta)
- AVerdadero
- BFalso
34Which of the following describe Prefoldin
- AJellyfish like structure
- BWith 6 coiled-coil beta sheets
- CWith 6 coiled-coil alpha helices
35There are 3.5 amino acid residues per helical turn of the coiled coil helices in Prefoldin (not 3.6)
- AVerdadero
- BFalso
36The subunits forming the dimerisation interface of the below molecule are what?
- AHydrophobic
- BHydrophillic
37Where do the non-native proteins bind to Prefoldin?
- AExposed hydrophobic residues in the distal ends of the 'tentacle'
- BExposed hydrophobic residues in the proximal ends of the 'tentacle'
- CExposed hydrophobic residues at the top of the 'tentacle'
Información
- Descripción
- (Protein Folding) Structural Basis for Biological Function Test sobre Constituative Chaperones, creado por gina_evans0312 el 20/12/2013.
- Autor
- gina_evans0312
- Idioma
- English
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- 1.373
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