Biochem 4000 - Lecture 4 PI

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  1. Difference between a turn, loop and strap
    • Turns - <6 Residues
    • Loops - 6+ Residues
    • Straps - 7+ Residues
  2. Types of helix
    310, alpha, pi
  3. What is this general structure?
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    reverse turn (type II)
  4. Types of reverse turn?
    • α - 5 i » i+4
    • β - 4 i » i+3
    • γ - 3 i » i+2
    • π(pi) - 6 i » i+5
  5. β-Hairpin
    Special case of reverse turn
  6. ω loop
    6-16 Residues, >7A (16+ Extended loops)
  7. When can torsion angles be in disallowed regions? (ramachandran)
    When the residue is glycine
  8. Most common type of reverse turn?
    Beta
  9. Common β-reverse turn angles
    ±30,±60, ±120 and 0 (glycine)
  10. Supersecondary structure
    Combinations of secondary structures in specific geometric arrangements
  11. What limits supersecondary conformations?
    Packing of R-groups
  12. Why do type II turns require glycine?
    Hydrogen bonding requires disallowed torsion angles
  13. β-hairpin
    Special case of a reverse turn
  14. β-hairpin turn
    Short loop segment joining two antiparalell β-strands.
  15. Favoured β-hairpin turns
    Types I' and II'
  16. Type I' beta turn residues
    Residue 1: Favours Gly, Asp or Asn

    Residue 2: Almost always Gly
  17. Type II' residues
    • Residue 1: Almost always Gly (left handed helix)
    • Residue 2: Small polar (Ser, Thr)
  18. 3 Residue β-hairpin structure
    • Single H-bond
    • Residue 1: Right handed helix conf.
    • Residue 2: Bridge
    • Residue 3: Left handed helix conf. (Gly, Asn, Asp)
  19. 4 Residue β-hairpin structure
    • Residue 1: Right handed helix conf.
    • Residue 2: Right handed helix conf.
    • Residue 3: Bridge
    • Residue 4: Left handed helix conf. (Gly, Asn, Asp)

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Author:
Ant
ID:
315793
Filename:
Biochem 4000 - Lecture 4 PI
Updated:
2016-02-19 20:58:20
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Biochemistry 4000
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Biochem 4000
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