Biol 196: Chapter 3 Terms

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Biol 196: Chapter 3 Terms
2013-02-18 23:38:36

Proteins, Carbohydrates, Lipids
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  1. Waxes?
    • Repels H2O
    • Formed by ester linkages between saturated long chain fatty acids and a saturated long chain alcohol.
  2. Steroids?
    • 4 ring structure (C,H)
    • part of membranes
    • Hormones
    • *Hydrophobic
  3. Vitamins?
    • Not synthesized in body, must acquire from diet
    • Vitamin: A,D,E,K = lipids
  4. Carotenoids?
    Traps light energy (plants and animals)
  5. Phospholipid Bilayers?
    • Sheet of Phospholipids two molecules thick, chemically stable
    • water excluded from the core!
  6. Amphipathic?
    Both Hydrophobic and Hydrophilic properties
  7. Phospholipids?
    same properties of triglycerides except any one phosphate containing compound replaces one fatty acid giving molecule amphipathic properties 
  8. Polyunsaturated Fatty Acids?
    2 double bonds near middle of hydrocarbon chain, causing a kink
  9. Unsaturated Fatty Acids?
    • Hydrocarbon chain consists of one or more double bonds
    • Bent prevents tight pack of fatty acids (plant oil)
  10. Saturated Fatty Acids?
    • Single hydrocarbon chain single bonds, no double bonds. 
    • Packed together (Animal Fat)
  11. Ester Linkages?
    • Covalent bond between carboxyl and hydroxyl groups, releases H2O 
    • Forms Triglycerides 
  12. Glycerol? 
    Small molecule contains 3 hydroxyl (OH) groups 
  13. Fatty acids?
    non polar hydrocarbon chain and a carboxyl group (COOH)
  14. Triglycerides?
    3 fatty acids and 1 molecule of glycerol
  15. Oils?
    Liquid at room temp (20C) 
  16. Fats?
    Solid in room temp (20C)
  17. Lipids?
    • Hydrophobic hydrocarbons
    • Insoluble in H2O because of Nonpolar bond
  18. Cellulose?
    • Structure in cell wall in plants (Beta- glycosidic linkages)
    • more stable
  19. Glycogen?
    • Energy storage for animals (Alpha- glycosidic linkages
    • stores glucose in muscle and liver
  20. Starch?
    Energy storage for plants (Alpha- glycosidic linkages)
  21. Glycosidic Linkage?
    Covalently bonded monosaccharides that construct sugar polymers by condensation reaction.
  22. Glucose?
    All living cells contain glucose, energy source releases stored energy produces H2O and CO2.
  23. Hexoses?
    • 6 carbon sugars
    • structural isomers; glucose and fructose
    • all have the formula: C6H12O6
  24. Pentose?
    • 5 carbon sugars
    • Backbone of DNA and RNA
  25. Polysaccharides?
    • Polymers; starch, glycogen and cellulose
    • Function: Energy Storage, Structure
    • * built from glucose
  26. Oligosaccharides?
    3-20 monosaccharides
  27. Disaccharides?
    • 2 monosaccarides linked covalently
    • EX: Sucrose -> glucose and fructose
  28. Monosaccharides?
    Simple Sugars; glucose, fructose, ribose
  29. Carbohydrates?
    • Association between H2O and C -> (CH2O)
    • Function: Energy storage and Transport, Carbon Skeleton (building block to build other molecules)
  30. Chaperones?
    Prevents inappropriate interaction and enhance appropriate interactions between protein binding
  31. Denature?
    Disrupt the secondary and tertiary structure to break down?
  32. Subunits?
    Two or more polypeptide chains, each folded into its own unique tertiary structure.
  33. Quaternary Structure?
    Multiple subunits (folded in its own tertiary structure) bind together and interact with each other
  34. Tertiary Structure?
    3-D shape, Interaction between R groups amino side chains determine tertiary structure, polypeptide chain is bent at specific sites and then folded.
  35. Beta Pleated Sheet?
    Polypeptide chains adjacent or parallel to one another, stabilized by H bonds between the N-H groups of one chain and the C=O groups on the other. 
  36. Alpha Helix?
    R.handed coil shape, H bonds form between H of the Amino group (N-H) and the O of the Carboxyl group (C=O)
  37. Secondary Structures?
    • Based H bonds between Amino Acids (carboxyl and amino groups) 
    • two basic types: 
    • 1. Alpha Helix
    • 2. Beta Pleated Sheet
  38. Primary Structure?
    • back bone of the polypeptide chain, consists of covalent bonds of (N-C-C) forming polypeptide chains.
    • * Not sole contributor to further levels of structure!
  39. C-Terminus?
    Free Carboxyl group, Last Amino Acids in the sequence
  40. N-Terminus?
    Free Amino group, 1st Amino Acid in the sequence.
  41. Peptide bond?
    The carboxyl group of one amino acid and Amino Group of another amino acid undergo condensation reaction, Links amino acids together.
  42. Sulfhydryl Group?
    Disulfied Bridge?
    • (SH group) terminal in cysteine that reacts with another cysteine side chain to form a covalent bond called a disulfide bridge (-S-S-).
    • DB helps determine how a polypeptide chain folds. 
  43. Special Cases?
    3 Amino Acids consists of Cysteine, Glycine, Proline (generally hydrophobic)
  44. Nonpolar hydrophobic amino acids?
    • 7 Amino Acids, non polar hydrocarbons (C-H) bonds, in H2O cluster together.
    • (No charge)
  45. Uncharged polar amino acids?
    5 Amino Acids that tend to for H bonds with H2O and polar charged substances. (hydrophilic)
  46. Charged Hydrophilic Amino Acid?
    3 consists of (+) charged and 2 (-) charged, attract H2O and opposite ions
  47. R group?
    • Defining, changing structure of the Amino Acid.
    • Determines 3-D structure thus the function of the protein
  48. Carboxyl group?
    • Acidic, Ionizes to form COO- and H+
    • (COOH -> COO-)
  49. Amino Group?
    • Basic, Accepts H+ to form NH3.
    • Gives up H+ in condensation reaction.
    • (NH2 -> NH3+)
  50. Alpha Carbon?
    First carbon attached to the functional group, asymmetrical, bonded to four different atoms or groups of atoms.
  51. Polypeptides?
    • single chain of covalently linked amino acids. (C-C-N)
    • *non functional must link up to other polypeptide, but if considered functional as a single unit it is referred to as a protein as well!
  52. Amino Acids?

    contain carboxyl and amino functional group and a side chain (R-group) attached to the same (alpha) carbon.
  53. Proteins?
    Polymers made up of 20 amino acids and consists of one or more polypeptide chain.
  54. Depolymerization?
    Break down into monomers or smaller units
  55. Hydrolysis reactions?
    H2O is added to polymers to breakdown into their monomers (opposite of Condensation reaction)
  56. Polymerization?
    Proccess of monomers reacting together to form a polymer
  57. Condensation (dehydration) reaction?
    factor of polymerization, H2O is released w/each covalent bond formed
  58. Optical Isomer?
    Mirror Image, occur when Carbon has 4 different atoms or groups of atoms attached to it. (asymmetrical carbon)
  59. Structural Isomer?
    Same amount of atoms, different how they are joined (structure)
  60. Isomer?
    Same chemical formula, diff structure
  61. Macromolecule?
    Polymers with molecular weight exceeding 1,000g/mol; refer to protein, carbohydrates, lipids.
  62. Polymer?
    molecule made up of monomers.
  63. Monomer?
    Covalently bonded molecules that make up a Polymer.