Constituative Chaperones

Descripción

(Protein Folding) Structural Basis for Biological Function Test sobre Constituative Chaperones, creado por gina_evans0312 el 20/12/2013.
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Test por gina_evans0312, actualizado hace más de 1 año
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Resumen del Recurso

Pregunta 1

Pregunta
Which of the following is not a role of the DNAK/Hsp70 superfamily?
Respuesta
  • Stabilise nascent polypeptides
  • Repaor heat shocked proteins
  • Preserve folding proteins
  • Protein transport
  • Protein degredation

Pregunta 2

Pregunta
Hsp70s (unlike DNAK's) do not require chaperones
Respuesta
  • True
  • False

Pregunta 3

Pregunta
What is the role of DNAJ/Hsp40 when combined with DNAK/Hsp70
Respuesta
  • ATPases
  • Kinases
  • Peptidyl propyl isomerases

Pregunta 4

Pregunta
DNAK/Hsp70 need NEF's in order to function
Respuesta
  • True
  • False

Pregunta 5

Pregunta
Where is the Hsp70/DNAK binding domain for ATP?
Respuesta
  • N-terminus
  • Core
  • C- terminus

Pregunta 6

Pregunta
Name the subdomains of the ATPase found in DNAK/Hsp70
Respuesta
  • 1A
  • 1B
  • 1C
  • 2A
  • 2B
  • 2C

Pregunta 7

Pregunta
What increases the ATPase activity of the ATP binding domain?
Respuesta
  • The binding of the substrate
  • Movement into an acidic compartment
  • DNAJ/Hsp40 binding
  • YDJ1 binding
  • SSA

Pregunta 8

Pregunta
The core substrate binding domain has an affinity for what?
Respuesta
  • Neutral, hydrophobic aa
  • Acidic, polar aa
  • Basic, polar aa

Pregunta 9

Pregunta
The C-terminus of DNAK/Hsp 70 acts as a 'lid' for the protein
Respuesta
  • True
  • False

Pregunta 10

Pregunta
When ATP is hydrolysed in DNAK/Hsp70, where does the C-terminus bind to?
Respuesta
  • The N-terminus
  • The core
  • It doesn't move at all
  • Over the bound substrate

Pregunta 11

Pregunta
Without the assistance of DNAJ/Hsp40, the ATPase in DNAK/Hsp70 works too slowly for the C-terminus to trap the bound substrate
Respuesta
  • True
  • False

Pregunta 12

Pregunta
Hsp70/DNAK's preferred binding pattern is 15 aa long
Respuesta
  • True
  • False

Pregunta 13

Pregunta
What are the 'Flanking' residues (1-4, 9-13) of Hsp70's preferred binding site made of?
Respuesta
  • Leu
  • Arg
  • Lys
  • Trp

Pregunta 14

Pregunta
The preferred residue for the -Core- of Hsp70's preferred binding site is Valine
Respuesta
  • True
  • False

Pregunta 15

Pregunta
What other residues can make up the 'core' of the preferred binding site/
Respuesta
  • Ile
  • Val
  • Phe
  • Tyr

Pregunta 16

Pregunta
How does this 'Preferred Binding Patter' for Hsp70 help direct the protein?
Respuesta
  • In properly folded proteins, the hydrophobic stretch is hidden, and so only nascent/denatured proteins have the exposed residues for Hsp70 to bind to
  • In nascent/denatured proteins, these hydrophobic residues will be added by Hsp40, so it can recognise them
  • Stretches with the core residues are removed during protein folding, so only nascent polypeptides have them

Pregunta 17

Pregunta
What is the role of the J domain in a Hsp40?
Respuesta
  • Contain the HPD peptide needed to boost Hsp40's ATPase
  • Gly/Phe rich linker for positioning
  • Dimerisation domain
  • Zn+ 'finger' for substrate binding

Pregunta 18

Pregunta
The role of the Gly/Phe rich linker does what?
Respuesta
  • Makes DNAJ/Hsp40 flexible enough to bind to its respective protein
  • Makes DNAJ/Hsp40 a more effective ATPase
  • Allows DNAJ/Hsp40 to locate its respective DNAK/Hsp70

Pregunta 19

Pregunta
The Zinc 'Finger' is for substrate binding
Respuesta
  • True
  • False

Pregunta 20

Pregunta
Which amino acids make up the HPD domain?
Respuesta
  • Histadine
  • Proline
  • Aspartate
  • Leucine
  • Glycine

Pregunta 21

Pregunta
The Znc finger of DNAJ/Hsp40 can interact with the nascent polypeptide and bring it to the DNAK/Hsp70
Respuesta
  • True
  • False

Pregunta 22

Pregunta
What is the sequence of the Zinc 'finger'?
Respuesta
  • CXXCXGXG
  • GXXGXCXC
  • GXXCXGXC
  • CXXGXCXG

Pregunta 23

Pregunta
The C-terminus of Hsp40 is for tetramerisation
Respuesta
  • True
  • False

Pregunta 24

Pregunta
What effect does the GEF factor binding have on the Hsp70/Hsp40 complex?
Respuesta
  • ADP is replaced with ATP
  • ATP is replaced with ADP
  • Hsp40 dissociates
  • Newly folded protein binds
  • Newly folded protein dissociates

Pregunta 25

Pregunta
When the substrate & Hsp40 bind to Hsp70, the GEF factor also binds
Respuesta
  • True
  • False

Pregunta 26

Pregunta
How is the nascent polypeptide transferred from the DNAJ site to the DNK site?
Respuesta
  • The G/F domain is flexible enough to bind to the DNAK site and pull it in for transfer
  • The J domain is pulled like a thread through the ATPase, bringing the two sites close enough together for transfer
  • The dimerisation of the DNAJ pulls the two sites close together

Pregunta 27

Pregunta
In which of the following is Prefoldin found?
Respuesta
  • Archea
  • Prokaryotes
  • Eukaryotes

Pregunta 28

Pregunta
Prefoldin can act as a substitute for Hsp70 if the organsim doesn't have the latter
Respuesta
  • True
  • False

Pregunta 29

Pregunta
Prefoldin is ATP dependent
Respuesta
  • True
  • False

Pregunta 30

Pregunta
Prefolding is a...
Respuesta
  • Dimer
  • Tetramer
  • Hexamer

Pregunta 31

Pregunta
What is the role of Preofoldin in Archea?
Respuesta
  • Captures nascent polypeptides and binds them to Gro-El
  • Captures nascent polypeptides and binds them to CCT
  • Captures nascent polypeptides and binds them to SSA

Pregunta 32

Pregunta
In Eukaryotes, prefoldin might be specific for the folding of what?
Respuesta
  • Actin/tubulin
  • CCT
  • Hsp40
  • Hsp70

Pregunta 33

Pregunta
In archea there are 6 Prefoldin genes (Grim1-6) in Eukaryotes there are 2 (Gimalpha and Gimbeta)
Respuesta
  • True
  • False

Pregunta 34

Pregunta
Which of the following describe Prefoldin
Respuesta
  • Jellyfish like structure
  • With 6 coiled-coil beta sheets
  • With 6 coiled-coil alpha helices

Pregunta 35

Pregunta
There are 3.5 amino acid residues per helical turn of the coiled coil helices in Prefoldin (not 3.6)
Respuesta
  • True
  • False

Pregunta 36

Pregunta
The subunits forming the dimerisation interface of the below molecule are what?
Respuesta
  • Hydrophobic
  • Hydrophillic

Pregunta 37

Pregunta
Where do the non-native proteins bind to Prefoldin?
Respuesta
  • Exposed hydrophobic residues in the distal ends of the 'tentacle'
  • Exposed hydrophobic residues in the proximal ends of the 'tentacle'
  • Exposed hydrophobic residues at the top of the 'tentacle'
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