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  1. what configuration do most amino acids have
    L shaped
  2. what two amino acids have secondary sterocenters
    isoleucine and thronine
  3. average pKa of acidic carboxyl group
  4. average pKa of basic NH3+ 
  5. peptide bond facts
    • trans
    • partial double bond
    • shorter than typical single bond but onger than double bonds
    • makes peptide bond group planar
  6. read peptides from
    • n terminal to c terminal
    • basic to acidic
  7. primary structure
    polypeptide chain, holds tertiary structure
  8. secondary structure
    hydrogen bonded arrangement of backbone of protein

    • free rotation bonds
    • C - N  (NH3)
    • C - C  (COO-)
  9. tertiary structure
    3-d arrangement of all atoms
  10. forces in tertiary structure (non covalent)
    • hydrogen bonds between polar side
    • hydrophobic interaction between nonpolar side
    • electrostatic attraction opposite charged side
    • electrostatic repulsion same charged side
    • covalent interaction disulfide bonds
  11. quatinary structure
    • arrangement of monomers subunits
    • noncovalent interactions
  12. A helix
    • right handed coil
    • 3.6 amino acids per turn
    • repeat distance is 5.4 A
    • R groups point outward
  13. factors that disrupt a-helix
    • proline creates a bend
    • electrostatic repulsion by proximity of several like charged side chains
    • steric crowding proximity of bulky side chains
  14. what can be on its own plane during a peptide bond
  15. amino acids found in reverse turns
    glycine and proline
  16. supersecondary stuctures
    combination of a-helix and b-sheets
  17. positive cooperativity
    function of hemoglobin, makes it easier to absorb oxygen as more is absorbed (allosteric).
  18. allosteric behavior
    as one molecule is bound it becomes easier to bind more
Card Set:
2013-10-09 01:23:46

chpt 3 and 4
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