December 14th Bio Test

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  1. Enzymes
    • Most are proteins
    • Speed up chem reactions and bind to specific substrates
    • Thee binding of a substrate w/ an enzyme causes a change in the enzyme's shape and reduces the activation energy of the reaction
    • Ends in -ase
    • organic catalyst: speed up reaction without changing itself, has C and H
    • contains a nonprotein part and active site
  2. Dehydrogenase
    Enzyme that removes hydrogen
  3. Proteinase (protease) and lipase
    Breaks down protein, breaks down lipids
  4. Catalyst
    • a substance that speeds up reaction rate
    • organic catalyst: both C and H
  5. Cofactor
    a non-protein chemical compound that is bound to a protein and is required for the protein's biological activity. These proteins are commonly enzymes, and cofactors can be considered "helper molecules" that assist in biochemical transformations.
  6. Coenzyme
    • They cannot by themselves catalyze a reaction but they can help enzymes to do so. In technical terms, coenzymes are organic nonprotein molecules that bind with the protein molecule (apoenzyme) to form the active enzyme (holoenzyme).
    • ex: some vitamins
  7. Active site
    where the substrate binds in an enzyme-substrate complex
  8. Denaturation
    • disruption and degradation of secondary or terciary protein structure
    • caused by heat, a strong acid, etc.
    • ex: an egg being cooked
  9. Substrate
    the compound that binds with its complementary enzyme
  10. Enzyme-substrate complex
    Substrate bound to enzyme, unit called this
  11. 2 enzyme-substrate models
    • 1) lock and key model
    • -lock fixed, substrate specificity
    • 2) induced fit model
    • -enzyme will change shape when it binds to the substrate
  12. Factors affecting enzyme activity
    • 1) temperature
    • -optimum temp is approx 36 C (upside down parabola)
    • 2)pH
    • -most enzymes fairly neutral, except pepsin in your stomach has pH of 2
    • 3) enzyme concentration
    • -plateau (sharp)
    • 4) substrate concentration
    • -plateau (rounded)
  13. Disulfide bond
    A type of strong covalent bond found in tertiary protein structure
  14. Hemoglobin
    • Has 4 polypeptide chains
    • Disease called sickle-cell enemia makes otherwise rounded blood cells cresent shaped
    • hemoglobin is altered, so it clumps
    • 6th terms isnt val (nonpolar), its glu (polar, acidic)
  15. Primary protein structure
    • Amino acids, linear sequence
    • in protein or polypeptide
  16. Secondary protein structure
    • Hydrogen bonds form peptide backbone
    • -alpha helix is twisted
    • -beta plated is folded
  17. Tertiary protein structure
    • folding, determined by interactions of R (variable) group
    • -bonds possible: Hydrogen, ionic, disulfide
  18. Quaternary protein structure
    arrangement of 2 plus polypepetide chains into multisubunit molecule
  19. Peptide bonds
    • linkage in amino acids
    • -formed by dehydration synthesis
    • -hydrolysis breaks this bond
  20. N-C terminal
    describes how protein folds (tertiary)
  21. Nutrient test lab
    • iodine-starch
    • benedicts-glucose
    • biuret-protein
  22. Catalase lab
    catalyzes hydrogen peroxide to form oxygen and hydrogen
  23. Amino acids
    • dipolar ions in water
    • amino group (-NH3+) and carboxyl group, r group
  24. carboxyl group
    • acidic
    • -think carbon with the double bonded oxygen, single OH
    • in trigylcerides, amino acids
  25. polypeptide chain
    Chain of amino acids that are peptide-bonded
  26. Inorganic vs organic
    • organic: both H and C
    • inorganic: anything else
  27. Hydrogen bond
    force of attraction between hydrogen atom with a partial positive charge and another O or N with a partial or full negative charge
  28. Ionic bonds
    • one atom gives up an electron
    • positive attracted to minus
  29. Covalent bonds
    two atoms share electrons
  30. Glycosidic bonds
    any bond that includes one carbohydrate molecule being synthesized to another molecule thru dehydration synthesis
  31. Ester bonds
    • bond between glycerol and fatty acid (so in trigycleride)
    • formed by dehydration synthesis
  32. Adhesion
    • attraction, holds molecules of diff substances together
    • -ex: water and glass
  33. Cohesion
    • attraction, holds molecules of a single substance together
    • -ex: water
  34. Capillary action
    • rise of liquids in small narrow tubes
    • -ex: sticking up straw in a milkshake
    • -water up stem of plant
  35. Surface tension
    • -a measure of the inward force at the surface of any liquid that can form hydrogen bonds
    • -ex: miniscus in a column
    • -caused by hydrogen bonding
    • -cohesion vs adhesion
  36. pH, acid/base
    • pH
    • -hydrogen ion concentration (negative log)
    • -Acids have a pH less than 7, taste sour, proton donor
    • -Bases have a pH greater than 7, feel slippery, proton acceptor
  37. Pentose
    • sugar with 5 carbons
    • monosaccharide
  38. Carbohydrates
    • most abundant compound in nature
    • often ends is -ose
    • composed of C, H, O
    • (CH2O)n
    • H:O is 2:1
  39. Isomer
    same molecular formula, diff structural formula
  40. Monosaccharide and polysaccharides
    • glucose and glucose is maltose
    • glucose and fructose is sucrose
    • glucose and galactose is lactose
  41. glucose (and isomers)
    Galactose and manose isomers
  42. Ribose
    sugar in RNA
  43. Alpha and beta glucose
    • alpha: OH down (we can digest)
    • beta: OH up
  44. Hydroxyl group
    • -OH bonded to amino acids
    • hydrophilic
    • tendency to form hydrogen bonds
    • diatomic ion with a single negative electronic charge
    • anything with a hydroxyl group is an alcohol
  45. Starch
    • the means by which plants utilize carbs as an energy source
    • we cant digest
  46. Glycogen
    • the means by which animals utilize carbs as an energy source
    • store energy
  47. Cellulose
    • a carbohydrate
    • plants use for structure
  48. Lipids functions
    • store energy (fat)
    • insolation
    • cushioning
    • cell membrane
    • sterol precursors of hormones

    • insoluable
    • H:O greater than 2:1
  49. Triglycerides
    Three fatty acids, one glycerol
  50. Unsaturated/saturated fats
    • Unsaturated- double bonds, liquid at room temp, oils, healthy, kinks
    • saturated-single bonds, solid at room temp, solids, unhealthy, no kinks
  51. Phospholipids
    • major component on cell membranes
    • composition: fatty acids, phosphate, choline tail, w/glycerol backbone
    • -phosphate with FA chain
  52. Hydrophilic/hydrophobic
    • phospholipid
    • head (phosphate) hydrophilic
    • fatty acid tail hydrophobic
  53. Sterol
    • cholesterol is a subset
    • 4 fused rings
    • precursor to hormones
  54. Hydrogenation
    • process of making unsaturated into saturated
    • -ex: how margarine is made
    • -lasts longer
  55. Proteins (and functions)
    • Functions
    • 1) enzymes, the biochem catalysts
    • 2) storage and transport of biochem molecules
    • 3) Physical cell support and shape (tubulin, actin, collagen)
    • 4) Mechanical movement (flagella, mitosis, muscles)

    Glycogen stores energy
  56. Glycine
    Amino acid, if R group is H
  57. Glycerol
    Type of alcohol
Card Set
December 14th Bio Test
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