Biology 196 Chapter 3 Class 1.2

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Biology 196 Chapter 3 Class 1.2
2012-06-06 05:27:29

Summer course 06/05/12
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  1. Organic Molecules
    Any chemical compound containing carbon
  2. Tetravalence
    • Makes large complex organic molecules possible
    • 4 valence electrons, share with important life atoms
  3. Carbon Skeletons (Backbones)
    • Straight, branched, ring
    • Can contain other atoms (O, N)
    • Double bonds= 2 electron pairs
    • Triple bonds= 3 electron pairs
  4. Double Bonds
    2 electron pairs
  5. Triple Bonds
    3 electron pairs
  6. Hydroxyl Group
    • Polar
    • H bonds with O (--OH)
  7. Alcohol
    -ol suffix
  8. Carbonyl Group
    • Consists of O atom joined to the C skeleton by a double bond
    • (--C=O)
  9. Aldehyde
    • Located at end of skeleton.
    • Important in building molecules in energy-releasing reactions
  10. Ketone
    • Not located at end of skeleton
    • Important in carbohydrates and energy reactions
  11. Carboxyl Group
    • C double bonded to an O along with another single bond to an OH group
    • Acidic
  12. Amino Group
    • Consists of N atom attached to 2 H atoms that is attached to the C skeleton
    • Basic
  13. Sulfhydril Group
    Consist of an S atom bound to an H and attached to a C skeleton
  14. Thiols
    Name of sulfhydril compound
  15. Phosphate Group
    Consists of P atom bound to 4 O atoms (3 with single bonds, 1 with a double bond)
  16. Hydrocarbon
    A compound containing only carbon and hydrogen atoms
  17. Hydrophobic
    • Water hating
    • Uncharged and nonpolar groups of atoms
  18. Hydrophilic
    Water loving
  19. Isomers
    Molecules with same molecular formula, different structures, different chemical properties because of shape
  20. Structural Isomers
    Molecules made up of same kinds/numbers of atoms, but bonded differently
  21. Optical Isomers
    Two isomers that are mirror images of each other.
  22. Monomers
    Small molecules used to form polymers
  23. Polymers
    • Consist of many similar or identical building blocks linked by covalent bonds
    • Monomers repeated over and over
  24. Condensation
    • Monomers assemble into large molecules
    • Covalent bonds formed
    • Releases water
  25. Hydrolysis
    • Reaction disassembles monomers
    • Covalent bond between monomers is broken
    • Need water to complete reaction
  26. Protein
    Polymers of amino acids connected in a specific way (polypeptide)
  27. Protein Functions
    • Structural (keratin, collagen)
    • Nutrient storage (yolk)
    • Transport (hemoglobin)
    • Catalysis (enzymes: speed up chemical reactions) *biggest function
    • Defense (antibodies: immune systems)
    • Hormones (insulin)
    • Movement (actin, myosin)
  28. Polypeptide
    Large molecule of many amino acids joined by peptide bonds (protein)
  29. Amino Acids
    Form polypeptides after joined by dehydration reaction
  30. R-Group
    • Side chain
    • Determine unique characteristics of a specific amino acid
  31. Charged-Hydrophilic Amino Acids
    • Acids and bases
    • Attracts ions of opposite charges
  32. Polar-Hydrophilic Amino Acids
    Polar but uncharged R-groups that form H-bonds with other groups
  33. Hydrophobic Amino Acids
    Nonpolar hydrophobic side chains
  34. Special Amino Acids
    Glycine (no asymmetric C), Proline (has modified R, forms ring), Cysteine (terminal SH group)
  35. Peptide Bond
    Resulting covalent bond
  36. Primary Structure
    Unique sequence of amino acids
  37. Secondary Structure
    • Hydrogen bonds at regular intervals along the polypeptide backbone with some specific amino acids.
    • Alpha helices (coils)
    • Beta sheets (pleats)
  38. Tertiary Structure
    Interactions among R groups and between R groups and the polypeptide backbone
  39. Quarternary Structure
    Aggregation of two or more polypeptide subunits (collagen, hemoglobin)
  40. Alpha Helix
    Right handed coils
  41. Beta Sheet
    alignment of one part with another by Hydrogen bonds (pleats)
  42. Disulfide Bridge
    Covalent bonds between Cysteine residues
  43. Denaturing
    Unraveling of a protein by disrupting the forces that maintain protein shape
  44. Chaperones
    • Important in proper folding and maintenance of the 3D structure of proteins
    • In heat-shock response protect protein for short period when temps are elevated
  45. Chaperonins
    Higher order structure that can refold denatured proteins.

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