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Molecular Chaperones in Bacteria, Yeast & Mammals

gina_evans0312 22 questions

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Questions in this quiz (22)

  1. 1What is the main role of a molecular chaperone?
    1. AAssist in the folding of other proteins
    2. BAssist in the unfolding of other proteins
    3. CAssist in the assembly of other proteins
    4. DAssist in the disassembly of other proteins
  2. 2Chaperone proteins are permanent parts of the proteins they fold
    1. ATrue
    2. BFalse
  3. 3Why are chaperone proteins necessary?
    1. ASome proteins have complex folding pathways,
    2. BSome proteins are inherently soluble
    3. CUseful for multimeric assembly
    4. DSo many proteins folding and interacting mean some need help
  4. 4Name the role of the domain highlighted in bacterial trigger factorImage for question 4
    1. APPIase domain
    2. BInteracts with polypeptide as it comes off the ribosome
    3. CBinds to L23 of the ribosome
  5. 5The highlighted domain of Bacterial trigger factor binds to L23 of the ribosomeImage for question 5
    1. ATrue
    2. BFalse
  6. 6The bacterial ribosome and bacterial trigger factor form a complex, so the protein is folded as it comes off the ribosome
    1. ATrue
    2. BFalse
  7. 7The N-domain of the bacterial trigger factor bind to what subunit of what size ribosome?
    1. AL23
    2. BL24
    3. CL25
    4. D50s
    5. E40s
    6. F30s
  8. 8After the protein interacts with the T.F, it may interact with what proteins?
    1. ADNAK
    2. BDNAJ
    3. CDNAL
    4. DGro-EL
    5. EGro-ER
  9. 9What percent of proteins can fold unaided after interacting with DNAK/J?
    1. A70%
    2. B65%
    3. C75%
  10. 1010-15% of proteins need to use the lidded protein chaperone syastem
    1. ATrue
    2. BFalse

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Description
Structural Basis for Biological Function (Protein Folding) Quiz on Molecular Chaperones in Bacteria, Yeast & Mammals, created by gina_evans0312 on 20/12/2013.
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