Bio 220 - Chapter 2 Molecular Interactions

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Bio 220 - Chapter 2 Molecular Interactions
2013-02-02 03:45:22
Bio 220 Chapter

Bio 220 - Chapter 2 Molecular Interactions
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  1. the basic unit of matter
  2. composed of protons, neutrons, electrons
  3. What determines the the element?
    the number of protons
  4. The number of protons is the same as the...
    Atomic number
  5. What is located in the nucleus?
    protons and neutrons
  6. What is located in the cloud around the nucleus?
  7. the number of protons + the average number of neutrons in the element =
    atomic mass
  8. the number of protons equals the number of electrons in a...
    neutral atom
  9. an element with a different number of neutrons than the protons...
  10. If an atom gains or loses an electron it becomes
    an Ion of the same element
  11. If an atom gains or loses a proton it becomes
    a different element
  12. If an atom gains or loses neutrons it becomes
    an Isotope of the same element
  13. If elements are in the same ROW on the periodic table they
    have the same number of electron shells
  14. If elements are in the same COLUMN on the periodic table they
    have the same number of electrons in the outermost shell
  15. Isotopes emit...
  16. the weight of an element
    atomic mass
  17. Octet rule
    atoms prefer that the outermost shell has 8 electrons
  18. shell 1 of the orbitals contains
    2 electrons
  19. shell 2 and shell 3 of the orbitals may contain
    up to 8 electrons
  20. cations
    positive charge
  21. anions
    negative charge
  22. strongest chemical bond
  23. chemical bond where atoms stick together as long as no H2O is present
  24. chemical bond with weak attractive forces
  25. chemical bond that is small, weak, nuclei have gravitational pull that holds them together, mostly seen in DNA
    Van der Waals
  26. Two elements that share electrons
    Shared pair = Covalent bond
  27. a positive end and negative end (opposing poles)
  28. electrons evenly shared (no opposing poles)
  29. anything polar likes...
  30. Nonpolar covalent bonds do not like...
  31. Water loving
  32. Water fearing
  33. Fat lover that is also hydrophobic
  34. Fat fearing
  35. Properties of water
    • surface tension (water beading)
    • high heat capacity
    • excellent solvent
    • location of many chemical reactions
    • ice is less dense than water
  36. The body's set point
  37. pH is the measure of the concentration of:
    H+ within a solution
  38. H+ interferes with
    Hydrogen bonds and van der Waals forces (causes cells to breakdown)
  39. What builds in the body during metabolism and exercise
  40. The more acidic pH the ____ the number
  41. Which atom is very good at sharing electrons
  42. organic molecules are based on...
    carbon atoms
  43. Carbons make ? bonds
    4 bonds - every carbon must have 4 "sticks"
  44. functional groups change
    the chemical properties of the molecule to melecules that have different functions
  45. Function of Carboxyl group (sugars)
    drops off H+ molecule and makes acidic
  46. Function of Hydroxyl group (alcohols)
    makes hydrophilic
  47. Function of Amino group (proteins) - Nitrogens are unique to this group
    accepts H+ from solution and acts as a buffer
  48. Function of Phosphate group
    adds energy to cells and makes acidic
  49. Order of amino acids - genes tell which amino acids to go where
    Primary structure
  50. What the amino acids look like when early folding takes place is the:
    secondary structure
  51. Early folding secondary structure of amino acids (looks like)
    • coil
    • alpha helix
    • beta pleated sheets
  52. The "R" group or side chain group does what?
    a changeable group that will push amino acids around and cause a change in the shape
  53. Building blocks of carbohydrates
    • monosaccharides remove H2O becomes
    • disaccharide removes H2O becomes
    • polysaccharide
  54. Biological function of carbohydrates
  55. Building blocks of lipids
    • Triglycerides / fatty acids
    • (hydrophobic)
  56. Biological function of lipids
    • Energy storage
    • protection
    • insulation
    • signaling
    • membrane structure
    • cushioning
  57. Building blocks of Nucleic acids
    DNA/RNA (Nucleotides - ATP)
  58. Biological function of Nucleic acids
    • Genetic storage/transfer
    • energy transfer
  59. Building blocks of proteins
    • Chains of Amino acids (polymer)
    • Monomers>polymers
    • Peptide bonds (Nitrogen and carboxylic acid)
  60. Biological function of proteins
    depends on its structure.

    Protein disruption will not bond with its ligand
  61. 3D shape of protein: globular or fibrous, is which stage
    Tertiary structure
  62. Once the protein is composed of multiple polypeptide subunits
    Quaternary structure
  63. Things denature H+ bonds causing them to lose tertiary structure and proteins unfold:
    • pH changes
    • temperature - Heat
    • too much Na+
  64. Name the 3D shapes of protein tertiary structures
    coils, pleats, and connectors
  65. Why does the shape of proteins matter?
    active sites for binding
  66. Shape change happens then protein goes back to original shape (like a handshake)
    induced fit
  67. The location of the interaction on the protein is called
    • binding site
    • active site
  68. Binding site is molecular complementary means
    only some or one ligand that a protein will interact with
  69. a molecule that binds to a protein
  70. an enzyme that binds to a protein
  71. Selective nature of the protein for a ligand
  72. The degree of attraction between a protein and the ligand
  73. Ligands that act as competitive inhibitors
  74. Ligands that act as competitive mimics
  75. Multiple versions of a protein that exist in different forms in different areas of the body
  76. proteins may be inactive until another molecule acts on it
    • activation
    • -proteolytic (cut off a little piece of it)
    • -cofactor
  77. changes the ability of the ligand to bind or change the activity of the protein
  78. Name the types of modulators
    • chemical modulators
    • antagonists
    • competitive inhibitors
    • allosteric modulators
    • covalent modulators
  79. cells regulate the amount of protein by
    • up-regulation
    • down-regulation

    "supermarket checkout lines"
  80. When the max of a protein is used
  81. max rate in which the protein is saturated and can't do job faster