Biology Lecture 1

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Biology Lecture 1
2014-02-27 11:25:32
Biology Lecture

intro level bio
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  1. the universal solvent
    Takes up 70 to 80 percent of a cell's mass
    Polar molecules that can hydrogen bond
  2. water's ability to ______ allows it stay liquid at room temp.
    This ability also provides strong cohesive forces between water molecules.
    Hydrogen bonding
    Strong cohesive forces, provided by hydrogen bonding, squeeze this molecule away from water and causes them to aggregate.
    hydrophobic molecules
  4. Water loving molecules that dissolves easily in water
    hydrophilic molecules
  5. Most macromolecules of living cells are broken apart with the addition of water. This process is called _________.
  6. Most macromolecules of living cells are formed with the removal of water
  7. any biological molecule that has low solubility in water and high solubility in non-polar organic solvents.
    a lipid
  8. six major groups of lipids
    fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes
  9. The building blocks for most complex lipids.
    They are long chains of carbons truncated at one end by a carboxylic acid.
    Usually an even number of carbons with the max being 24 in humans.
    Can be saturated or unsaturated.
    Fatty acids
  10. Fatty acids that possess only single carbon-carbon bonds
    Saturated fatty acids
  11. Fatty acids that contain one or more carbon-carbon double bonds
    Unsaturated fatty acids
  12. This lipid is constructed from a three carbon backbone called glycerol.
    their function is to store energy. They may also function to provide thermal insulation and padding to an organism
    triacylglycerols or triglycerides or fats and oils
  13. These fat cells are specialized cells whose cytoplasm contains almost nothing but triglycerides
  14. This lipid is also built from a glycerol backbone but a polar phosphate group replaces one of the fatty acids. This lipid is amphipathic
  15. This marcomolecule is built from a chain of amino acids linked together by peptide bonds. They are sometimes referred to as polypeptides.
  16. The number and sequence of amino acids in a polypeptide is called ______
    the primary structure
  17. Once the primary structure is formed, the single chain can twist in to  an _____________ or lie along side itself and form a  __________
    alpha helix, beta-pleated sheet
  18. Alpha helix and beta pleated sheets are a part of which structure?
    Secondary structure
  19. This Structure is the 3-dimensional shape that is formed when the peptide chain curls and folds.
    Tertiary structure
  20. When two of more polypeptide chains bind together, they form this structure.
    Quaternary structure
  21. When the conformation is disrupted, the protein is said be _______.
  22. This macromolecule is made off of carbon and water with the empirical formula C(H2O).
    aka sugars or saccharides
  23. Five and six carbon carbohydrates are the most common in nature. The six carbon carbohydrate called _____ is the most commonly occurring sugar of all the six carbon sugars.
  24. Animals eat _______ linkage but only bacteria break down _______ linkage
    alpha, beta
  25. glucose and starch have _____ linkage so they can be consumed by animals.
  26. Cellulose has _____ linkage, so animals that consume cellulose must have certain type of bacteria in their stomach to digest it.
  27. This carbohydrate is made from glucose. They are found in all animal cells and have large amount in muscle and liver cells. have alpha linkages
  28. This macromolecule is composed of three components: a five carbon sugar
                        a nitrogenous base
                        a phosphate group
  29. Nucleotides form polymers to create _____________ such as DNA and RNA
    Nucleic acid
  30. The type of bonds nucleotides use to form nucleic acids
    phosphodiester bonds
  31. This nucleotide is the source of readily available energy for the cell
    ATP (adenosine triphosphate)
  32. This nucleotide is an important component in many second messenger systems.
    cyclic AMP
  33. These nucleotides are the coenzymes involved in the Krebs cycle
    NADH and FADH2
  34. The dissolved inorganic ions inside and outside the cell. They assist in the transport of substances entering and exiting the cell.
  35. These globular protiens function as a catalyst for reactions by lowering the activation energy thus speeding up the reaction
  36. what is the reactant(s) upon which an enzyme works called?
  37. The position on the enzyme where the substrate binds
    active site
  38. Enzymes are designed to work only on a specific substrate or group  of closely related substrate. This design is called:
    an example is the lock and key theory and induce fit model.
    enzyme specificity
  39. This type of enzyme specificity states that the active site of the enzyme has a specific shape that only fits a specific substrate.
    the lock and key theory
  40. This type of enzyme specificity states the shape of both the enzyme and the substrate are altered upon binding.
    the induced fit model
  41. In order to reach their optimal activity, many enzymes require a non-protein component called ____________. They are usually minerals or coenzymes.
  42. These organic molecules are vitamins that are considered cofactors
  43. What are agents that bind covalently to enzymes and disrupt their function?
    irreversible inhibitors
  44. This inhibitor competes with the substrate by bining reversibly with noncovalent bonds to the active site. Once bonded, the substrate is blocked from bonding.
    competitive inhibitors
  45. This inhibitor binds noncovalently to an enzyme at a spot other that the active site and change the conformation of the enzyme. There is no competition between inhibitor and and substrate.
    noncompetitive inhibtors
  46. The modification of the enzyme configuration resulting from the binding of an activatio or inhibitor at a specific binding site on the enzyme.
    Allosteric interactions
  47. This phenomenon provides a shut down mechanism for a series of enzymatic reactions when that series has produced a sufficient amount of product.
    negative feedback
  48. This phenomenon occrs when the product returns to activate te enzyme.
    Postive feedback (tends to occur less than negative feedback)
  49. The change of the enzyme configuation after the binding of feedback inhibitors
    allosteric regulation
  50. The suffix for enzymes are:
  51. This is all cellular chemical reactions. It includes anabolism (molecular synthesis) and catabolism (molecular degradation)
  52. respiration in which oxygen is not required
    anaerobic respiration
  53. the first stage of anaerobic and aerobic respiration. It is the series of reactions that break down a six carbon glucose molecule into 3-carbon molecule of pyruvate. other important products in 2 ATP and 2 NADH
  54. the reaction of glycolysis occur in this fluid portion of living cells
    the cytosol
  55. This anaerobic respiration includes the process of glycolysis, the reduction of pyruvate to ethanol or lactic acid and the oxidation of NADH to NAD+
    Yeast produce ethanol and muscle cells produce lactic acid as waste product as well as CO2
    aerobic respiration
  57. The products of glycolysis will move to this part of the mitochondria if oxygen is available and the cell is capable of aerobic respiration
    matrix of a mitodchondrion
  58. This membrane is not very permeable. Pyruvate moves through it using facilitated diffusion. Once pyruvate is passed the membrane and is inside the matrix, it is converted into acetyl CoA in a reaction that produces NADH and CO2
    Inner Mitochondrial Membrane
  59. This is a coenzyme that transfers two carbons from pyruvate to the four carbon oxaloacetic acid to begin the Kreb cycle aka the citric acid cycle.
    ACEtyl CoA
  60. Each turn of this cycle produces 1 ATP, 3 NADH and 1 FADH2
    Kreb Cycle or the Citric Acid Cycle
  61. Aerobic respiration  produces about this many net ATP