Biochem 4000 - Structures

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  1. 2-Residue beta hairpin (type I')
    • Residue 1: Left handed helix
    • Residue 2: Glycine
  2. 2-Residue beta hairpin (type II')
    • Residue 1: Gly
    • Residue 2: Small, polar
  3. 3-Residue beta hairpin
    • Residue 1: Right handed helix
    • Residue 2: Helix-sheet bridge
    • Residue 3: Left handed helix (Gly, Asn, Asp)
  4. 4 Residue beta hairpins
    • Residue 1: Right handed helix
    • Residue 2: Right handed helix
    • Residue 3: Helix-sheet bridge
    • Residue 4: Left handed helix (Gly, Asn, Asp)
  5. β-meander
    Sheets connected by a series of long loops
  6. Other beta
    • Ω-Loops
    • Regular turns
    • Reverse turns
  7. Beta corner
    • 2-Residue disruption/bulge (beta hairpin)
    • 90° change in direction
  8. 2-Residue αα hairpin
    • Residue 1: α-β bridge
    • Residue 2: Gly
  9. 3-Residue αα hairpin
    • Residue 1: α-β bridge (caps first helix)
    • Residue 2: Left handed helix (caps both helices)
    • Residue 3: β-strand
  10. 4-Residue αα hairpin (conformation 1)
    • Residue 1: Bridging
    • Residue 2: Left handed helix
    • Residue 3: β-strand
  11. 4-Residue αα hairpin (conformation 2)
    • Residue 1: β-strand
    • Residue 2: Bridging
  12. αα corner
    • Two helices connect by a short loop (right-handed)
    • Residue 1: Small (Ala, Gly) (cap first helix)
    • Residue 2: Hydrophobic
    • Residue 3: Small, polar (Ser, Asp) (cap second helix)
  13. Helix-turn-helix
    • Ca2+ binding
    • 12 Residue loop (contains Gly6, Asp and Glu)
    • Pairs
  14. Helix-loop-helix
    DNA binding
  15. βαβ motif -
    • Paralell β-sheet
    • Paralell helix (perp. to strands)
    • Right handed
  16. Alpha bundle topology
    • Up and down
    • Paralell
    • Mixed
  17. Helix packing interactions
    • I+4 -> i+3 Parallel 23°
    • i+4 -> i+4 Orthoganol 52°
    • i+4 -> i+1 Orthoganol 105°
  18. Aligned β-sandwich, sheet angled
    -20° - -50°
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317505
Card Set
Biochem 4000 - Structures
Description
Biochem
Updated
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