Biomed final review 3b

  1. What are the four levels of protein structure?
    Primary - the sequence of amino acids

    Secondary - how that sequence if folded (a:helix, B: pleated sheet)

    Tertiary - how helices or sheets are arranged in three dimensions.

    Quaternary - arrangement of 3D structures into whole protein.
  2. Define Primary Structure
    the order in which amino acids are strung together with peptide bonds.
  3. The primary structure may be twisted or folded into a
    Secondary structure
  4. The Secondary structure of a protein is the
    coiling or folding of its polypeptide chains.
  5. a-helix
    "spiral staircase"
  6. Hair is an a-helical structure formed from the protein
    Keratin; Keratin is made up of three a-helices twisted together in a cable.
  7. Many proteins that span the membrane are made up of
    a-helices with the -R groups of hydrophobic (non-polar) amino acids associating with the hydrophobic lipids of the cell membrane and the -R groups of hydrophilic (polar) amino acids forming the pore.
  8. "B"- pleated sheets
    are found in many proteins in nature (such as spider silk) but are less common in human proteins.
  9. Protein Structure illustrated.  Helices, pleated, amino acids that don't have secondary structure.
    a-helices are represented as coils

    B-pleated sheets are represented as arrow (arrow points amino)

    Amino acids that don't have secondary structure are threads
  10. Tertiary structures within proteins are
    formed when separated chains, or different a-helices, or other parts of chains are joind together into a larger, folded structure.
  11. Types of atomic interactions leading to Tertiary structure
    Ionic bonds

    Hydrophobic interactions

    Van der Waals interactions ("shapes" of molecules fit each other like puzzle pieces)

    Disulfide bridges (are formed between cysteines. Cysteine is the only amino acid with an -SH group.Hydrogen bonds
  12. Heme group
    an iron-containing group which holds onto the oxygen molecule.
  13. Hemoglobin
    the oxygen-carrying protein of the blood.
  14. The proper function of hemoglobin depends critically on
    primary, secondary, tertiary and quaternary structure.  Any alteration in the protein at any of these levels causes disease
  15. Primary, secondary and tertiary structure, combine together into a
    quaternary structure.
  16. Chemical reactions either absorb or _________ energy.
  17. Substance undergoing reaction =
  18. Enzyme names almost always end in
  19. What splits the disaccharide sucrose into glucose and fructose?
  20. Graphic module 3 obj. 33
    Define enzyme. Demonstrate factors that affect enxyme activeity, including denaturation, and interpret graphs showing the effects of various factors on the rate of enzyme-catalyzed reactions. p.159-164
  21. What do "squiggles" represent
    High energy bonds   ATP
  22. Cellular pathways that require energy are adapted to use
    ATP as their energy source
  23. What is used as the energy currency for the cell?
  24. What is the secret of ATP?
    High-energy phosphate bonds
  25. Forms of cellular energy.  What are the types of energy?
    • Electrical
    • Heat
    • Potential (chemical)
    • Radiant
  26. What bionergetic event does elctrical produce?
    Nerve inpulses
  27. What bioenergetic event does heat produce?
    Cellular chemical reactions
  28. What bioenergetic event does mechanical produce?
    Muscle contractions
  29. What bioenergetic event does potential (chemical) produce?
    Energy-rich covalent bonds
  30. What bioenergetic event does radiant produce?
    photosynthesis in plants
Card Set
Biomed final review 3b
Biomed final review 3b