2 pleated sheet 37 extended 120 and 120

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Unformatted text preview: ropensity scale •  •  •  •  •  •  •  –  stabilizing AA: alanine, leucine –  destabilizing AA: glycine (good on end), proline Secondary Structures – Beta Sheet •  H bond with groups from different strand •  Parallel, anCparallel, or mixed sheets •  translaCon/residue: 3.2 Å (pleated sheet), 3.7 Å (extended) •  Φ = - 120° and Ψ = 120° •  Cα atoms alternate above and below the plane of the sheet •  side chains point alternately above and below the sheet •  amphipathic sheets, hydrophobic residue pa`ern: i, i+2 Structural MoCf – Coiled- Coil Parallel AnC- Parallel •  oken parallel, but can be anCparallel •  repeaCng distance: 140 Å •  lek handed •  hydrophobic residues pa`ern: i, i+7 residues (heptad repeat) •  at helices interface: hydrophobic residues to allow packing (someCmes polar residues to determine the register) •  at border of interface: charged residues to define register and orientaCon of the helices Structural MoCf – Others •  Helices Packing –  Ridges into grooves –  i, i+4 - - i,i+4 ridges à༎ 5...
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This note was uploaded on 03/05/2014 for the course MCB 100A taught by Professor Kuryian during the Fall '09 term at University of California, Berkeley.

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