Biochem Protein Folding

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Author:
Ant
ID:
291589
Filename:
Biochem Protein Folding
Updated:
2014-12-14 20:29:51
Tags:
Biochem
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Description:
Protein Folding
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  1. What conditions are required for spontaneous protein folding?
    Physiological Conditions
  2. What level of peptide structure dictates folding?
    Primary
  3. How would you denature and renature a protein?
    • Denature:
    • - Betamercaptoethanol
    • - 8M Urea
    • Renature:
    • - Dialyze urea
    • - Add O2
    • - pH 8.0
  4. What protein activity did RNAase have after renaturation?
    100%
  5. Why are helices and motifs common structural elements?
    Effective space filling (not hydrogen bonding)
  6. What are two factors affecting protein folding?
    • Internal Residues
    • Hydrophobic Forces
  7. Do proteins fold randomly, (do they just sort of clump together)?
    No, they fold hierarchically
  8. What are some properties of T4 Lysozyme?
    • - Destroys bacterial cell walls by hydrolyzing peptidoglycan linkage
    • - 164 Residues
    • - Easy to Crystallize
    • - Monomeric
  9. What effect do surface residues have on protein folding?
    Little to no effect
  10. Is the protein ruined if you insert slight changed into primary structure?
    No, there is some flexibility as to protein structure
  11. In what organisms are unfolded proteins found?
    "Higher" organisms
  12. What are some features of natively unfolded proteins?
    • - Low sequence complexity
    • - DNA binding, cell signalling
    • - May change shape upon binding
  13. What is Levinthal's equation?


    - For n residues
  14. Briefly outline Stopped flow
    • - Two tanks, supplying a mixer
    • - Stop by "stopping syringe"
    • - Visualize with detector
  15. What are some methods of detecting protein folding?
    • - Absorbance - Least effective
    • - Circular Dichroism - Circular polarized light
    • - Fluorescence - Dyes
  16. What occurs on the interval t>3ms in protein folding?
    • - Rapid formation of hydrophobic core
    • ¬† - Radius close to native state
    • - Most secondary structure formed (internal)
  17. What occurs on the interval 5>t>1000ms in protein folding?
    • - Subdomains folded
    • - Side chains are mobile
  18. What occurs on the interval t>3ms in protein folding?
    • - Final chains fold
    • - Water molecules expelled
  19. What is a foldon?
    • A hierarchical and marginally stable microstructure in folding.
    • - Resemble native state
    • - Form during translation (co-translational)
    • - Sequential growth into native state

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