amino acid

  1. primary structure
    linear sequence of amino acids bounded by a polypeptide bond
  2. what are residues
    amino acids that no longer posses ionizable amino or carboxyl groups
  3. secondary structure
    • the three dimensional arrangement of proteins as a result of folding. Bound by a hydrogen bond.
    • two types of structure: a-helix, b-sheet
  4. why is proline known as a helix breaker
    its small structure does not allow for h-bonding.
  5. a-helix
    spiral arrangement with 3.6 amino acids residues per turn and R side chains extending outward
  6. describe b-sheet
    flat, extended arrangement either parallel or antiparallel
  7. describe tertiary structure
    • the entire conformation of a complete polypeptide chain
    • conformation is driven by hydrophobic effect where hydrophobic residues tend to be inside and hydrophillic residues tend to be outside
  8. describe quarternary structure
    the assembly of two or more tertiary structures producing a complete functional protein
  9. what is familiar parkinson's disease
    when there is a lack of alpha synuclein (protein) production which is necessary for the release of neurotransmitters in the synaptic vesicles in the brain.
  10. what is sickle cell anemia
    caused by single point mutation, when glutamic acid (polar) is converted to valine (nonpolar) produces a sickle shaped hemoglobin structure
Card Set
amino acid
amino acid, residues, primary, secondary, tertiary and quarternary structure