Constituative Chaperones

gina_evans0312
Quiz by gina_evans0312, updated more than 1 year ago
gina_evans0312
Created by gina_evans0312 almost 7 years ago
1286
0

Description

Structural Basis for Biological Function (Protein Folding) Quiz on Constituative Chaperones, created by gina_evans0312 on 12/20/2013.

Resource summary

Question 1

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

Question 2

Question
Hsp70s (unlike DNAK's) do not require chaperones
Answer
  • True
  • False

Question 3

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

Question 4

Question
DNAK/Hsp70 need NEF's in order to function
Answer
  • True
  • False

Question 5

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

Question 6

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

Question 7

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

Question 8

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

Question 9

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

Question 10

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

Question 11

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

Question 12

Question
Hsp70/DNAK's preferred binding pattern is 15 aa long
Answer
  • True
  • False

Question 13

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

Question 14

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

Question 15

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

Question 16

Question
How does this 'Preferred Binding Patter' for Hsp70 help direct the protein?
Answer
  • 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

Question 17

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

Question 18

Question
The role of the Gly/Phe rich linker does what?
Answer
  • 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

Question 19

Question
The Zinc 'Finger' is for substrate binding
Answer
  • True
  • False

Question 20

Question
Which amino acids make up the HPD domain?
Answer
  • Histadine
  • Proline
  • Aspartate
  • Leucine
  • Glycine

Question 21

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

Question 22

Question
What is the sequence of the Zinc 'finger'?
Answer
  • CXXCXGXG
  • GXXGXCXC
  • GXXCXGXC
  • CXXGXCXG

Question 23

Question
The C-terminus of Hsp40 is for tetramerisation
Answer
  • True
  • False

Question 24

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

Question 25

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

Question 26

Question
How is the nascent polypeptide transferred from the DNAJ site to the DNK site?
Answer
  • 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

Question 27

Question
In which of the following is Prefoldin found?
Answer
  • Archea
  • Prokaryotes
  • Eukaryotes

Question 28

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

Question 29

Question
Prefoldin is ATP dependent
Answer
  • True
  • False

Question 30

Question
Prefolding is a...
Answer
  • Dimer
  • Tetramer
  • Hexamer

Question 31

Question
What is the role of Preofoldin in Archea?
Answer
  • 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

Question 32

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

Question 33

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

Question 34

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

Question 35

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

Question 36

Question
The subunits forming the dimerisation interface of the below molecule are what?
Answer
  • Hydrophobic
  • Hydrophillic

Question 37

Question
Where do the non-native proteins bind to Prefoldin?
Answer
  • 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'
Show full summary Hide full summary

Similar

Protein Folding- The Basics
gina_evans0312
Chaperonins
gina_evans0312
Heat Shock Proteins
gina_evans0312
Supersecondary Structures & Energy Changes
gina_evans0312
Molecular Chaperones in Bacteria, Yeast & Mammals
gina_evans0312
Glycosylation
gina_evans0312
Properties of Chaperones
gina_evans0312
Molecular Motors- Helicases
gina_evans0312
Protein Structure Pt. 1
gina_evans0312
DNA-Protein Interactions 1
gina_evans0312
Motor Proteins- Myosin
gina_evans0312