CH-103 Chap 19

  1. Structural Protein; function and example:
    • Function: Provide structural components.
    • Collagen is in tendons and cartilage.
    • Keratin is in hair, skin, wool and nails.
  2. Contractile protein; function and example:
    • Function: Move muscles.
    • Myosin and actin contract muscle fibers.
  3. Transport protein; function and example:
    • Function: carry essential substances throughout the body.
    • Hemoglobin transports oxygen.
    • Lipoproteins transport lipids.
  4. Storage protein; function and example:
    • Function: Store nutrients.
    • Casein stores protein in milk. Ferritin stores iron in the spleen and liver.
  5. Hormone proteins; function and example:
    • Function: Regulate body metabolism and nervous system.
    • Insulin regulates blood glucose level.
    • Growth hormone regulates body growth.
  6. Enzyme protein; function and example:
    • Function: Catalyze biochemical reactions in the cells.
    • Sucrase catalyzes the hydrolysis of sucrose. Trypsin catalyzes the hydrolysis of proteins.
  7. Protection protein; function and example:
    • Function: Recognize and destroy foreign substances.
    • Immunoglobins stimulate immune responses.
  8. Every Amino acid has:
    • a central carbon atom bonded to an ammonium group.
    • a carboxylate group (--COO-).
    • a Hydrogen atom.
    • a side chain or R group.
  9. Nonpolar amino acids contain:
    • alkyl or aromatic R groups
    • this makes them hydrophobic.
  10. Polar amino acids contain:
    • Neutral
    • polar R groups such as hydroxyl (--OH), thiol (--SH) and amide (--CONH2).
    • these are hydrophylic.
  11. Acidic Amino acids contain:
    R groups that have carboxylate (--COO-).
  12. Basic amino acids contain:
    R groups that have ammonium (--NH3+).
  13. Describe the functional groups found in all alpha-Amino acids:
    all amino acids contain a carboxylate group and an ammonium group on the alpha chain.
  14. The use of electrical current to separate proteins or other charged molecules:
  15. The pH at which an amino acid exists as a zwitterion with a net charge of zero:
    isoelectric point.
  16. The combination of two or more amino acids joined by peptide bonds:
  17. The amide bond in that joins the carboxylate group of one amino acid with the ammonium group in the next amino acid:
    Peptide bond.
  18. Quaternary structure:
    a protein sttructure in which tow or more protein subunits form an active protein.
  19. Salt Bridge:
    The attraction between the ionized R groups of basic and acidic amino acids in the tertiary structure of a protein.
  20. Primary structure:
    The specific sequence of the amino acids in a protein.
  21. Secondary Structure:
    The formation of an alpha-helix, Beta-pleated sheet, or triple helix.
  22. Tertiary structure:
    The folding of the secondary structure of a protein into a compact structure that is stabilized by the interactions of R groups such as ionic and disulfide bonds.
  23. Triple helix:
    The protein structure found in collage consisting of three polypeptide chains woven together like a braid.
  24. Zwitterion:
    The dipolar form of an amino acid consisting of two oppositely charged ionic regions, --NH3+ and --COO-.
Card Set
CH-103 Chap 19
Amino Acids & Proteins